ArticleClinical and diagnostic laboratory immunology1998
Expression, structure, and location of epitopes of the major surface glycoprotein of Pneumocystis carinii f. sp. carinii.
Article in Clinical and diagnostic laboratory immunology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- β-Glucans Are Masked but Contribute to Pulmonary Inflammation During Pneumocystis Pneumonia.The Journal of infectious diseases · 2016Article
- Genome analysis of three Pneumocystis species reveals adaptation mechanisms to life exclusively in mammalian hosts.Nature communications · 2016Article
- Pneumocystis encodes a functional endo-β-1,3-glucanase that is expressed exclusively in cysts.The Journal of infectious diseases · 2015Article
- Functional characterization and localization of Pneumocystis carinii lanosterol synthase.Eukaryotic cell · 2010Article
- Geographical variation in serological responses to recombinant Pneumocystis jirovecii major surface glycoprotein antigens.Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases · 2009Article
- Biofilm formation by Pneumocystis spp.Eukaryotic cell · 2009Article
- Human immunodeficiency virus-infected patients with prior Pneumocystis pneumonia exhibit increased serologic reactivity to several major surface glycoprotein clones.Clinical and vaccine immunology : CVI · 2006Article
- Immunological features of Pneumocystis carinii infection in humans.Clinical and diagnostic laboratory immunology · 1999Review
- Identification of a putative precursor to the major surface glycoprotein of Pneumocystis carinii.Infection and immunity · 1998Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The major surface glycoprotein (MSG) of Pneumocystis carinii f. sp. carinii consists of a heterogeneous family of proteins that are encoded by approximately 100 unique genes. A genomic expression library was screened with a panel of MSG-specific monoclonal antibodies (MAbs) to identify conserved and rare epitopes. All of the antibodies reacted with epitopes that are encoded within the 5' end of MSG. The results from the expression screening identified antibodies that recognize highly conserved, moderately conserved, and rare epitopes. Four MAbs (MAbs RA-F1, RA-E7, RA-G10, and RB-E3) reacted with a maltose binding protein-MSG-B fusion protein ([MBP]MSG-B41-1065) by immunoblotting and enzyme-linked immunosorbent assay. Three of the MAbs (MAbs RA-F1, RA-G10, and RA-E7) reacted with the same continuous epitope that was localized to amino acids 278 to 290 of MSG-B. Comparison of the sequence of the RA-F1-, RA-G10-, and RA-E7-reactive epitope to the deduced amino acid sequences of multiple MSGs demonstrated that it is highly conserved. The reactivity of RB-E3 with MSG-B was shown to be dependent on amino acids 184 to 192, which may comprise a portion of a discontinuous epitope.
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