Characterization and functional analysis of a novel C-type lectin in blunt snout bream (

C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Liu, Yang [verfasserIn] Wang, Zuzhen [verfasserIn] Wang, Wenjun [verfasserIn] Liu, Bing [verfasserIn] Li, Chunfang [verfasserIn] Sun, Yuandong [verfasserIn] Cao, Jiri [verfasserIn] Xia, Kuanyu [verfasserIn] Yang, Moci [verfasserIn] Yan, Jinpeng [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	C-type lectin Antibacterial response Pattern recognition receptor

Übergeordnetes Werk:	Enthalten in: Fish & shellfish immunology - London : Elsevier, 1991, 140
Übergeordnetes Werk:	volume:140

DOI / URN:	10.1016/j.fsi.2023.108966

Katalog-ID:	ELV062109022

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024	7		\|a 10.1016/j.fsi.2023.108966 \|2 doi
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100	1		\|a Liu, Yang \|e verfasserin \|4 aut
245	1	0	\|a Characterization and functional analysis of a novel C-type lectin in blunt snout bream (
264		1	\|c 2023
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337			\|a Computermedien \|b c \|2 rdamedia
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520			\|a C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish.
650		4	\|a C-type lectin
650		4	\|a Antibacterial response
650		4	\|a Pattern recognition receptor
700	1		\|a Wang, Zuzhen \|e verfasserin \|4 aut
700	1		\|a Wang, Wenjun \|e verfasserin \|4 aut
700	1		\|a Liu, Bing \|e verfasserin \|4 aut
700	1		\|a Li, Chunfang \|e verfasserin \|4 aut
700	1		\|a Sun, Yuandong \|e verfasserin \|4 aut
700	1		\|a Cao, Jiri \|e verfasserin \|4 aut
700	1		\|a Xia, Kuanyu \|e verfasserin \|4 aut
700	1		\|a Yang, Moci \|e verfasserin \|4 aut
700	1		\|a Yan, Jinpeng \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Fish & shellfish immunology \|d London : Elsevier, 1991 \|g 140 \|h Online-Ressource \|w (DE-627)266877141 \|w (DE-600)1467514-6 \|w (DE-576)259270695 \|x 1095-9947 \|7 nnns
773	1	8	\|g volume:140
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912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_100
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_370
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912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
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912			\|a GBV_ILN_2232
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912			\|a GBV_ILN_2507
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
936	b	k	\|a 46.00 \|j Tiermedizin: Allgemeines \|q VZ
951			\|a AR
952			\|d 140

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author_variant	y l yl z w zw w w ww b l bl c l cl y s ys j c jc k x kx m y my j y jy
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allfields	10.1016/j.fsi.2023.108966 doi (DE-627)ELV062109022 (ELSEVIER)S1050-4648(23)00452-7 DE-627 ger DE-627 rda eng 630 VZ 22 ssgn 46.00 bkl Liu, Yang verfasserin aut Characterization and functional analysis of a novel C-type lectin in blunt snout bream ( 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish. C-type lectin Antibacterial response Pattern recognition receptor Wang, Zuzhen verfasserin aut Wang, Wenjun verfasserin aut Liu, Bing verfasserin aut Li, Chunfang verfasserin aut Sun, Yuandong verfasserin aut Cao, Jiri verfasserin aut Xia, Kuanyu verfasserin aut Yang, Moci verfasserin aut Yan, Jinpeng verfasserin aut Enthalten in Fish & shellfish immunology London : Elsevier, 1991 140 Online-Ressource (DE-627)266877141 (DE-600)1467514-6 (DE-576)259270695 1095-9947 nnns volume:140 GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 46.00 Tiermedizin: Allgemeines VZ AR 140
spelling	10.1016/j.fsi.2023.108966 doi (DE-627)ELV062109022 (ELSEVIER)S1050-4648(23)00452-7 DE-627 ger DE-627 rda eng 630 VZ 22 ssgn 46.00 bkl Liu, Yang verfasserin aut Characterization and functional analysis of a novel C-type lectin in blunt snout bream ( 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish. C-type lectin Antibacterial response Pattern recognition receptor Wang, Zuzhen verfasserin aut Wang, Wenjun verfasserin aut Liu, Bing verfasserin aut Li, Chunfang verfasserin aut Sun, Yuandong verfasserin aut Cao, Jiri verfasserin aut Xia, Kuanyu verfasserin aut Yang, Moci verfasserin aut Yan, Jinpeng verfasserin aut Enthalten in Fish & shellfish immunology London : Elsevier, 1991 140 Online-Ressource (DE-627)266877141 (DE-600)1467514-6 (DE-576)259270695 1095-9947 nnns volume:140 GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 46.00 Tiermedizin: Allgemeines VZ AR 140
allfields_unstemmed	10.1016/j.fsi.2023.108966 doi (DE-627)ELV062109022 (ELSEVIER)S1050-4648(23)00452-7 DE-627 ger DE-627 rda eng 630 VZ 22 ssgn 46.00 bkl Liu, Yang verfasserin aut Characterization and functional analysis of a novel C-type lectin in blunt snout bream ( 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish. C-type lectin Antibacterial response Pattern recognition receptor Wang, Zuzhen verfasserin aut Wang, Wenjun verfasserin aut Liu, Bing verfasserin aut Li, Chunfang verfasserin aut Sun, Yuandong verfasserin aut Cao, Jiri verfasserin aut Xia, Kuanyu verfasserin aut Yang, Moci verfasserin aut Yan, Jinpeng verfasserin aut Enthalten in Fish & shellfish immunology London : Elsevier, 1991 140 Online-Ressource (DE-627)266877141 (DE-600)1467514-6 (DE-576)259270695 1095-9947 nnns volume:140 GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 46.00 Tiermedizin: Allgemeines VZ AR 140
allfieldsGer	10.1016/j.fsi.2023.108966 doi (DE-627)ELV062109022 (ELSEVIER)S1050-4648(23)00452-7 DE-627 ger DE-627 rda eng 630 VZ 22 ssgn 46.00 bkl Liu, Yang verfasserin aut Characterization and functional analysis of a novel C-type lectin in blunt snout bream ( 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish. C-type lectin Antibacterial response Pattern recognition receptor Wang, Zuzhen verfasserin aut Wang, Wenjun verfasserin aut Liu, Bing verfasserin aut Li, Chunfang verfasserin aut Sun, Yuandong verfasserin aut Cao, Jiri verfasserin aut Xia, Kuanyu verfasserin aut Yang, Moci verfasserin aut Yan, Jinpeng verfasserin aut Enthalten in Fish & shellfish immunology London : Elsevier, 1991 140 Online-Ressource (DE-627)266877141 (DE-600)1467514-6 (DE-576)259270695 1095-9947 nnns volume:140 GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 46.00 Tiermedizin: Allgemeines VZ AR 140
allfieldsSound	10.1016/j.fsi.2023.108966 doi (DE-627)ELV062109022 (ELSEVIER)S1050-4648(23)00452-7 DE-627 ger DE-627 rda eng 630 VZ 22 ssgn 46.00 bkl Liu, Yang verfasserin aut Characterization and functional analysis of a novel C-type lectin in blunt snout bream ( 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish. C-type lectin Antibacterial response Pattern recognition receptor Wang, Zuzhen verfasserin aut Wang, Wenjun verfasserin aut Liu, Bing verfasserin aut Li, Chunfang verfasserin aut Sun, Yuandong verfasserin aut Cao, Jiri verfasserin aut Xia, Kuanyu verfasserin aut Yang, Moci verfasserin aut Yan, Jinpeng verfasserin aut Enthalten in Fish & shellfish immunology London : Elsevier, 1991 140 Online-Ressource (DE-627)266877141 (DE-600)1467514-6 (DE-576)259270695 1095-9947 nnns volume:140 GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 46.00 Tiermedizin: Allgemeines VZ AR 140
language	English
source	Enthalten in Fish & shellfish immunology 140 volume:140
sourceStr	Enthalten in Fish & shellfish immunology 140 volume:140
format_phy_str_mv	Article
bklname	Tiermedizin: Allgemeines
institution	findex.gbv.de
topic_facet	C-type lectin Antibacterial response Pattern recognition receptor
dewey-raw	630
isfreeaccess_bool	false
container_title	Fish & shellfish immunology
authorswithroles_txt_mv	Liu, Yang @@aut@@ Wang, Zuzhen @@aut@@ Wang, Wenjun @@aut@@ Liu, Bing @@aut@@ Li, Chunfang @@aut@@ Sun, Yuandong @@aut@@ Cao, Jiri @@aut@@ Xia, Kuanyu @@aut@@ Yang, Moci @@aut@@ Yan, Jinpeng @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	266877141
dewey-sort	3630
id	ELV062109022
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV062109022</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230927084026.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230824s2023 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.fsi.2023.108966</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV062109022</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S1050-4648(23)00452-7</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">630</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">22</subfield><subfield code="2">ssgn</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">46.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Liu, Yang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Characterization and functional analysis of a novel C-type lectin in blunt snout bream (</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2023</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. 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The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. 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spellingShingle	Liu, Yang ddc 630 ssgn 22 bkl 46.00 misc C-type lectin misc Antibacterial response misc Pattern recognition receptor Characterization and functional analysis of a novel C-type lectin in blunt snout bream (
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topic_title	630 VZ 22 ssgn 46.00 bkl Characterization and functional analysis of a novel C-type lectin in blunt snout bream ( C-type lectin Antibacterial response Pattern recognition receptor
topic	ddc 630 ssgn 22 bkl 46.00 misc C-type lectin misc Antibacterial response misc Pattern recognition receptor
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title	Characterization and functional analysis of a novel C-type lectin in blunt snout bream (
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title_full	Characterization and functional analysis of a novel C-type lectin in blunt snout bream (
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author_browse	Liu, Yang Wang, Zuzhen Wang, Wenjun Liu, Bing Li, Chunfang Sun, Yuandong Cao, Jiri Xia, Kuanyu Yang, Moci Yan, Jinpeng
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title_sort	characterization and functional analysis of a novel c-type lectin in blunt snout bream (
title_auth	Characterization and functional analysis of a novel C-type lectin in blunt snout bream (
abstract	C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish.
abstractGer	C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish.
abstract_unstemmed	C-type lectins, one of the pattern recognition receptors (PRRs), play significant roles in innate immune responses through binding to the pathogen-associated molecular patterns (PAMPs) presented on surfaces of microorganisms. Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish.
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title_short	Characterization and functional analysis of a novel C-type lectin in blunt snout bream (
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author2	Wang, Zuzhen Wang, Wenjun Liu, Bing Li, Chunfang Sun, Yuandong Cao, Jiri Xia, Kuanyu Yang, Moci Yan, Jinpeng
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up_date	2024-07-06T18:24:49.285Z
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Here, a novel C-type lectin (named as MaCTL) from blunt snout bream (Megalobrama amblycephala) was cloned and characterized. The open reading frame (ORF) of MaCTL is 573 bp long encoding a putative protein of 190 amino acids (aa), which contains a typical feature of signal peptide at 1–23 aa, a characteristic CRD domain at 45–178 aa and a WND/EPN motif that is required for carbohydrates-binding specificity. Phylogenetic analysis indicated that MaCTL is a novel member of CTL family and possessed the highest similarity to that of grass carp (92.11%). The qRT-PCR analysis revealed that MaCTL expressed widely in all examined normal tissues, including heart, liver, spleen, kidney, head-kidney, gill, intestine and muscle, with the higher expression in the spleen, liver and muscle. The expression of MaCTL in spleen was significantly elevated, peaking at 9 h and 6 h after LPS stimulation and Aeromonas hydrophila challenge, respectively, suggesting its association with involvement in innate immune response. The recombinant MaCTL protein (rMaCTL) agglutinated markedly both Gram-positive (Staphylococcus aureus) and Gram-negative bacteria, including Escherichia coli, Vibrio anguillarum, Vibrio vulnificus and Aeromonas hydrophila, in a Ca2+-dependent manner. Meanwhile, rMaCTL showed the binding effects on the five bacteria and four carbohydrates, such as glucose, surose, LPS and PGN. Moreover, rMaCTL could remarkably inhibit the growth of three types of bacteria in vitro. Overall, the results obtained above demonstrated firmly that MaCTL binds to carbohydrates on the surface of diverse pathogens as a PRR and elicits antimicrobial responses, which shed new light on a better understanding of antibacterial functions of CTLs in teleost fish.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">C-type lectin</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Antibacterial response</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Pattern recognition receptor</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Zuzhen</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Wenjun</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Liu, Bing</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Chunfang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sun, Yuandong</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cao, Jiri</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Xia, Kuanyu</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yang, Moci</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yan, 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Characterization and functional analysis of a novel C-type lectin in blunt snout bream (

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