Rat-derived Pneumocystis carinii lysed with sodium deoxycholate catalysed the incorporation of uridine diphosphoglucose into an insoluble polymer. This enzyme activity was present in both the pellet and the supernatant when the P. carinii preparations were centrifuged. The polymer whose production was catalysed by the supernatant was examined by mass spectrometry and found to be an alpha 1----4 glucan, which is either unbranched or has relatively few branches. Polymer formation was completely inhibited by the addition of alpha amyloglucohydrolase to the supernatant. Polymer formation in the pellet of deoxycholate P. carinii preparations, unlike that in the supernatant, was partially resistant to alpha amyloglucohydrolase. The soluble glucan synthase activity in the supernatant was stable for more than 30 h at room temperature and was approximately 50 times more active on a cell-to-cell basis than the supernatant from deoxycholate preparations of the yeast Saccharomyces cerevisae.

Pneumocystis carinii is an opportunistic pathogen of man, carried as a commensal in healthy subjects. It frequently causes a fatal pneumonia in the immunosuppressed host. It is a major complication of HIV-1 infection in man (AIDS). Using surface radioiodination of rat-derived P. carinii trophozoites obtained from in vitro culture, a major surface glycoprotein (gp120) has been identified. The glycoprotein exhibits adherent behavior similar to that of the intact organism. Purification of gp120 by conventional methods was unsuccessful as the glycoprotein irreversibly bound to numerous column matrices. A combination of gel chromatography and hydroxyapatite chromatography in sodium dodecylsulfate was utilized to purify the glycoprotein. Some preliminary characterization of the glycoprotein is presented.

The Journal of ProtozoologyVolume 36, Issue s1 p. 41s-43s Characterization of Pneumocystis carinii Monoclonal Antibodies M.S. BOGUCKI, M.S. BOGUCKI Section of Infectious DiseaseSearch for more papers by this authorJ.A. FISHMAN, J.A. FISHMAN Section of Infectious Disease, Massachusetts General Hospital, Boston, MA 02114, USA.Search for more papers by this authorJ.A. RADDING, J.A. RADDING Yale Macarthur Center for Molecular Parasitology, Departments of Internal MedicineSearch for more papers by this authorM.Y.K. ARMSTRONG, M.Y.K. ARMSTRONG Epidemiology and Public Health, Yale University School of Medicine, New Haven, CT 06510Search for more papers by this authorF.F. RICHARDS, F.F. RICHARDS Yale Macarthur Center for Molecular Parasitology, Departments of Internal MedicineSearch for more papers by this author M.S. BOGUCKI, M.S. BOGUCKI Section of Infectious DiseaseSearch for more papers by this authorJ.A. FISHMAN, J.A. FISHMAN Section of Infectious Disease, Massachusetts General Hospital, Boston, MA 02114, USA.Search for more papers by this authorJ.A. RADDING, J.A. RADDING Yale Macarthur Center for Molecular Parasitology, Departments of Internal MedicineSearch for more papers by this authorM.Y.K. ARMSTRONG, M.Y.K. ARMSTRONG Epidemiology and Public Health, Yale University School of Medicine, New Haven, CT 06510Search for more papers by this authorF.F. RICHARDS, F.F. RICHARDS Yale Macarthur Center for Molecular Parasitology, Departments of Internal MedicineSearch for more papers by this author First published: May 1989 https://doi.org/10.1111/j.1550-7408.1989.tb05824.xAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL No abstract is available for this article. LITRATURE CITED 1 Armstrong, M.Y.K. & Richards, F.F. 1989 J. Protmool. This issue. 2 Graves, D.C., McNabb, S.J.N., Ivey, M.H., &, Worley, M.A. 1986. Infect. Immun. 51: 125– 133. 3 Graves, D.C., McNabb, S.J.N, Worley, M.A., Downs, T.D., &, Ivey, M.H. 1986. Infect. Immun., 54: 96– 103. 4 Hockfield, S. 1987. Science, 237: 67– 70. 5 Lee, C-H., Bolinger, CD., Bartlett, M.S., Kohlcr, R.B., Wilde, C.E. & Smith, J.W. 1986. J. Clin. Microbiol., 23: 505– 508. 6 Radding, J. A., Armstrong, M.Y.K., Bogucki, M.S. & Richards, F.F. 1989. J. Protozool. This issue. 7 Walzer, P.D. & Linke, M.J. 1987. J. Immunol., 138: 2257– 2265. 8 Walzer, P.D., Stanforth, D., Linke, MJ. & Cushion, M.Y. 1987. Exp. Parasitol., 63: 319– 327. Volume36, Issues1May 1989Pages 41s-43s ReferencesRelatedInformation

Radioiodination of rat-derived Pneumocystis carinii obtained from an in vitro culture demonstrated the presence of a major surface glycoprotein (gp120). The glycoprotein was of the high mannose type. It exhibited adherence properties similar to those observed in the intact organism. Under nonreducing conditions, it existed as an aggregate with a molecular weight in excess of 2 x 10(6). Surface aggregating behavior and adherent quality prevented isolation of the glycoprotein by conventional methods. The glycoprotein was purified by chromatography on hydroxyapatite in the presence of sodium dodecyl sulfate under reducing conditions.

The complete primary structures of two variant specific glycoproteins (VSGs) of the nannomonad Trypanosoma (N.) congolense are presented. These coat proteins subserve the function of antigenic variation. The secondary structure potentials of both VSGs have been calculated. The amino acid sequences and secondary structure potentials of these VSGs have been compared with the primary structures and secondary structure potentials of several Trypanosoma brucei complex VSGs. In homologous regions, the T. brucei complex VSGs show a pattern of sharply contrasting secondary structure potentials. It has been suggested previously that this pattern gives rise to different folding structures in different members of this polygene protein family. Thus, different short regions of the polypeptide sequence are exposed as antigenic "caps" on the solvent-exposed surface of intact trypanosomes. A sharply contrasting secondary structure potential pattern is also found in regions of the two T. congolense VSGs. However, there is little homology of primary structure between each of the two T. congolense VSGs and any member of the T. brucei complex VSG polygene family whose primary structure has been determined.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTFurther studies on the structural requirements for synthetic peptide chemoattractantsRichard J. Freer, Alan R. Day, Jeffrey A. Radding, Elliott Schiffmann, S. Aswanikumar, Henry J. Showell, and Elmer L. BeckerCite this: Biochemistry 1980, 19, 11, 2404–2410Publication Date (Print):May 27, 1980Publication History Published online1 May 2002Published inissue 27 May 1980https://pubs.acs.org/doi/10.1021/bi00552a019https://doi.org/10.1021/bi00552a019research-articleACS PublicationsRequest reuse permissionsArticle Views263Altmetric-Citations163LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts