Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii
Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had bee...
Ausführliche Beschreibung
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| Autor*in: |
Broomall, Kathleen R. [verfasserIn] Morris, Randal E. [verfasserIn] Walzer, Peter D. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1998 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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2007 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: The journal of eukaryotic microbiology - Oxford [u.a.] : Wiley-Blackwell, 1954, 45(1998), 3, Seite 0 |
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volume:45 ; year:1998 ; number:3 ; pages:0 |
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10.1111/j.1550-7408.1998.tb04537.x |
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| 520 | |a Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. | ||
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10.1111/j.1550-7408.1998.tb04537.x doi (DE-627)NLEJ243278454 DE-627 ger DE-627 rakwb Broomall, Kathleen R. verfasserin aut Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Immunoelectron microscopy Morris, Randal E. verfasserin aut Walzer, Peter D. verfasserin aut Smulian, A. George oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 45(1998), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:45 year:1998 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1998.tb04537.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1998 3 0 |
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10.1111/j.1550-7408.1998.tb04537.x doi (DE-627)NLEJ243278454 DE-627 ger DE-627 rakwb Broomall, Kathleen R. verfasserin aut Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Immunoelectron microscopy Morris, Randal E. verfasserin aut Walzer, Peter D. verfasserin aut Smulian, A. George oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 45(1998), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:45 year:1998 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1998.tb04537.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1998 3 0 |
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10.1111/j.1550-7408.1998.tb04537.x doi (DE-627)NLEJ243278454 DE-627 ger DE-627 rakwb Broomall, Kathleen R. verfasserin aut Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Immunoelectron microscopy Morris, Randal E. verfasserin aut Walzer, Peter D. verfasserin aut Smulian, A. George oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 45(1998), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:45 year:1998 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1998.tb04537.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1998 3 0 |
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10.1111/j.1550-7408.1998.tb04537.x doi (DE-627)NLEJ243278454 DE-627 ger DE-627 rakwb Broomall, Kathleen R. verfasserin aut Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Immunoelectron microscopy Morris, Randal E. verfasserin aut Walzer, Peter D. verfasserin aut Smulian, A. George oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 45(1998), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:45 year:1998 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1998.tb04537.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1998 3 0 |
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10.1111/j.1550-7408.1998.tb04537.x doi (DE-627)NLEJ243278454 DE-627 ger DE-627 rakwb Broomall, Kathleen R. verfasserin aut Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Immunoelectron microscopy Morris, Randal E. verfasserin aut Walzer, Peter D. verfasserin aut Smulian, A. George oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 45(1998), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:45 year:1998 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1998.tb04537.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1998 3 0 |
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zymolyase treatment exposes p55 antigen of pneumocystis carinii |
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Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii |
| abstract |
Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. |
| abstractGer |
Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. |
| abstract_unstemmed |
Rats exposed to Pneumocystis carinii mount antibody responses to a broad band migrating on western blot with an apparent molecular weight of 45-55 kDa. One antigen within this band, designated p55, is uniformly recognized by P. carinii exposed rats. Although the gene encoding the p55 antigen had been previously cloned, the location of this antigen within the organism was unknown. Prior attempts to localize the protein were unsuccessful. A monospecific polyclonal antiserum raised against a carboxyl-terminai 15-oligomer peptide yielded specific reactivity with a single 55 kDa band on a western blot of P. carinii. Using this antiserum, little to no reactivity could be detected with P. carinii organisms by immunofluorescence assay (IIFA). However, zymolyase treatment of P. carinii dramatically increased the intensity and proportion of organisms reactive by IFA. Zymolyase, an enzyme with β-1,3 glucanase activity, has previously been shown to remove the electron dense outer layer of the P. carinii cell wall, exposing an electron lucent layer. Immunoelectron microscopy performed on zymolyase treated organisms showed the majority of labeling occurs within the cell wall. |
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| title_short |
Zymolyase Treatment Exposes p55 Antigen of Pneumocystis carinii |
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http://dx.doi.org/10.1111/j.1550-7408.1998.tb04537.x |
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| author2 |
Morris, Randal E. Walzer, Peter D. Smulian, A. George |
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Morris, Randal E. Walzer, Peter D. Smulian, A. George |
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| doi_str |
10.1111/j.1550-7408.1998.tb04537.x |
| up_date |
2024-07-06T04:55:52.083Z |
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7.401967 |