Open AccessLipoproteome screening of the Lyme disease agent identifies inhibitors of antibody-mediated complement killing
Author(s) -
Michael J. Pereira,
Beau Wager,
Ryan J. Garrigues,
Eva Gerlach,
Joshua D. Quinn,
Alexander S. Dowdell,
Marcia S. Osburne,
Wolfram R. Zückert,
Peter Kraiczy,
Brandon L. Garcia,
John M. Leong
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2117770119
Subject(s) - borrelia burgdorferi , biology , microbiology and biotechnology , lyme disease , complement system , borrelia , antibody , pathogen , treponema , virology , immunology , syphilis , human immunodeficiency virus (hiv)
Significance Spirochetal pathogens encode an abundance of lipoproteins that can provide a critical interface with the host environment.Borrelia burgdorferi , the model species for spirochetal biology, must survive an enzootic life cycle defined by fluctuations between vector (tick) and vertebrate host. WhileB. burgdorferi expresses over 80 surface lipoproteins—many of which likely contribute to host survival—theB. burgdorferi lipoproteome is poorly characterized. Here, we generated a platform to rapidly identify targets ofB. burgdorferi surface lipoproteins and identified two paralogs that confer resistance to antibody-initiated complement killing that may promote survival in immunocompetent hosts. This work expands our understanding of complement evasion mechanisms and points toward a discovery approach for identifying host–pathogen interactions central to spirochete pathogenesis.