Borrelia burgdorferi surface-located Lmp1 protein processed into region-specific polypeptides that are critical for microbial persistence.

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TitleBorrelia burgdorferi surface-located Lmp1 protein processed into region-specific polypeptides that are critical for microbial persistence.
Publication TypeJournal Article
Year of Publication2018
AuthorsZhuang, X, Yang, X, Altieri, AS, Nelson, DC, Pal, U
JournalCell Microbiol
Paginatione12855
Date Published2018 May 10
ISSN1462-5822
Abstract

One of the Borrelia burgdorferi virulence determinants, annotated as Lmp1, is a surface-exposed, conserved and potential multi-domain protein involved in various functions in spirochete infectivity. Lmp1 contributes to host-pathogen interactions and evasion of host adaptive immunity by spirochetes. Here we show that in diverse B. burgdorferi species, Lmp1 exists as distinct, region-specific and lower molecular mass polypeptides encompassing one or more domains, including independent N-terminal and middle regions and a combined middle and C-terminal region. These polypeptides originate from complex posttranslational maturation events, partly supported by a periplasmic serine protease termed as BbHtrA. While spirochete persistence in mice is independently supported by domain-specific Lmp1 polypeptides, transmission of B. burgdorferi from ticks to mammals requires essential contributions from both N-terminal and middle regions. Interference with the functions of Lmp1 domains or their complex posttranslational maturation events may aid in development of novel therapeutic strategies to combat infection and transmission of pathogens.

DOI10.1111/cmi.12855
Alternate JournalCell. Microbiol.
PubMed ID29749010
Grant ListR01 AI080615 / AI / NIAID NIH HHS / United States
R01 AI116620 / AI / NIAID NIH HHS / United States