Purification and initial characterization of a ferret pneumocystis carinii surface antigen

Francis Gigliotti; Leslie R. Ballou; Walter T. Hughes; Bernetta D. Mosley; Francis Gigliotti

doi:10.1093/infdis/158.4.848

Purification and initial characterization of a ferret pneumocystis carinii surface antigen

Francis Gigliotti, Leslie R. Ballou, Walter T. Hughes, Bernetta D. Mosley, Francis Gigliotti

School of Medicine

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Abstract

The purification and initial characterization of a ferret Pneumocystis carinii surface glycoprotein is described. Previous studies have demonstrated that passive administration of monoclonal antibody recognizing this glycoprotein reduces the severity of P. carinii pneumonitis in animal models of infection. This acidic glycoprotein (approximate isoelectric point, 5.0-5.7) contains both mannose (and/or glucose) and AT-acetyl-glucosamine residues. The cross-reactive surface antigen on P. carinii of human origin is also a mannose-(and/or glucose-) containing glycoprotein. Initial biochemical characterization of these surface molecules should aid in understanding the immunobiology of this organism and in developing reliable diagnostic assays for P. carinii pneumonitis.

Original language	English (US)
Pages (from-to)	848-854
Number of pages	7
Journal	Journal of Infectious Diseases
Volume	158
Issue number	4
DOIs	https://doi.org/10.1093/infdis/158.4.848
State	Published - Oct 1988

ASJC Scopus subject areas

Immunology and Allergy
Infectious Diseases

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title = "Purification and initial characterization of a ferret pneumocystis carinii surface antigen",

abstract = "The purification and initial characterization of a ferret Pneumocystis carinii surface glycoprotein is described. Previous studies have demonstrated that passive administration of monoclonal antibody recognizing this glycoprotein reduces the severity of P. carinii pneumonitis in animal models of infection. This acidic glycoprotein (approximate isoelectric point, 5.0-5.7) contains both mannose (and/or glucose) and AT-acetyl-glucosamine residues. The cross-reactive surface antigen on P. carinii of human origin is also a mannose-(and/or glucose-) containing glycoprotein. Initial biochemical characterization of these surface molecules should aid in understanding the immunobiology of this organism and in developing reliable diagnostic assays for P. carinii pneumonitis.",

author = "Francis Gigliotti and Ballou, {Leslie R.} and Hughes, {Walter T.} and Mosley, {Bernetta D.} and Francis Gigliotti",

note = "Funding Information: Received for publication 27 January 1988and in revised form 4 May 1988. This work was supported by grant AI-23302 from the National Institute of Allergy and Infectious Diseases and by the American Lebanese Syrian Associated Charities. Please address requests for reprints to Dr. Gigliotti at his present address: Department of Pediatrics, Division of Infectious Diseases, University of Rochester School of Medicine and Dentistry, Box 690, 601 Elmwood Avenue, Rochester, New York 14642. Copyright: Copyright 2016 Elsevier B.V., All rights reserved.",

year = "1988",

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doi = "10.1093/infdis/158.4.848",

language = "English (US)",

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AU - Ballou, Leslie R.

AU - Hughes, Walter T.

AU - Mosley, Bernetta D.

AU - Gigliotti, Francis

N1 - Funding Information: Received for publication 27 January 1988and in revised form 4 May 1988. This work was supported by grant AI-23302 from the National Institute of Allergy and Infectious Diseases and by the American Lebanese Syrian Associated Charities. Please address requests for reprints to Dr. Gigliotti at his present address: Department of Pediatrics, Division of Infectious Diseases, University of Rochester School of Medicine and Dentistry, Box 690, 601 Elmwood Avenue, Rochester, New York 14642. Copyright: Copyright 2016 Elsevier B.V., All rights reserved.

PY - 1988/10

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N2 - The purification and initial characterization of a ferret Pneumocystis carinii surface glycoprotein is described. Previous studies have demonstrated that passive administration of monoclonal antibody recognizing this glycoprotein reduces the severity of P. carinii pneumonitis in animal models of infection. This acidic glycoprotein (approximate isoelectric point, 5.0-5.7) contains both mannose (and/or glucose) and AT-acetyl-glucosamine residues. The cross-reactive surface antigen on P. carinii of human origin is also a mannose-(and/or glucose-) containing glycoprotein. Initial biochemical characterization of these surface molecules should aid in understanding the immunobiology of this organism and in developing reliable diagnostic assays for P. carinii pneumonitis.

AB - The purification and initial characterization of a ferret Pneumocystis carinii surface glycoprotein is described. Previous studies have demonstrated that passive administration of monoclonal antibody recognizing this glycoprotein reduces the severity of P. carinii pneumonitis in animal models of infection. This acidic glycoprotein (approximate isoelectric point, 5.0-5.7) contains both mannose (and/or glucose) and AT-acetyl-glucosamine residues. The cross-reactive surface antigen on P. carinii of human origin is also a mannose-(and/or glucose-) containing glycoprotein. Initial biochemical characterization of these surface molecules should aid in understanding the immunobiology of this organism and in developing reliable diagnostic assays for P. carinii pneumonitis.

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Purification and initial characterization of a ferret pneumocystis carinii surface antigen

Abstract

ASJC Scopus subject areas

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