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Contribution of Glycosylation to T Cell Responses Stimulated by RecombinantCryptococcus neoformansMannoprotein
Author(s) -
Charles A. Specht,
S H g,
Jennifer M. Dan,
Chrono K. Lee,
Stuart M. Levitz
Publication year - 2007
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 - 10.1086/520536
Subject(s) - cryptococcus neoformans , pichia pastoris , mannose , antigen , glycosylation , recombinant dna , microbiology and biotechnology , glycoprotein , biology , yeast , biochemistry , immunology , gene
Mannoproteins are major antigens driving T cell responses to the opportunistic fungus Cryptococcus neoformans. To investigate the role played by mannosylation, an immunoreactive cryptococcal mannoprotein was expressed recombinantly in E. coli and Pichia pastoris, resulting in unglycosylated and mannosylated proteins, respectively. The Pichia-derived antigen stimulated stronger major histocompatibility class II-restricted T cell responses. Moreover, responses were potently inhibited if the antigen was chemically deglycosylated or if mannose receptors were blocked with mannans. Thus, mannosylation is critical for optimal T cell responses to a fungal antigen and should be taken into account when vaccines to protect against mycoses are designed.

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