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Serologic Responses to Epitopes of the Major Surface Glycoprotein ofPneumocystis jiroveciDiffer in Human Immunodeficiency Virus–Infected and Uninfected Persons
Author(s) -
Kieran R. Daly,
Carl J. Fichtenbaum,
Reiko Tanaka,
Michael J. Linke,
Robert O’Bert,
Timothy D. Thullen,
Michele S. Hui,
A. George Smulian,
Peter D. Walzer
Publication year - 2002
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/341565
Subject(s) - virology , serology , epitope , immunology , glycoprotein , human immunodeficiency virus (hiv) , biology , antibody , medicine , genetics
The major surface glycoprotein (Msg) of Pneumocystis jiroveci (P. jiroveci) is important in the immunopathogenesis of Pneumocystis pneumonia (PcP), but is difficult to study in humans. We generated 3 overlapping recombinant Msg fragments (MsgA, MsgB and MsgC), and analyzed their reactivity with serum samples from 95 healthy blood donors and 94 human immunodeficiency virus (HIV)-infected persons. Reactivity to the Msg fragments varied with HIV infection and prior episodes of PcP but not with geographic origin. Recognition of MsgA was lower-and recognition of MsgB was significantly lower-in HIV(+) serum compared with donor serum. Serum samples from HIV-positive patients with prior PcP recognized MsgC more frequently than did serum samples from those without PcP. None of the serum samples drawn from 9 patients before they had developed PcP recognized MsgC. These data suggest that these novel recombinant proteins are useful for the analysis of antibody responses to Msg.

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