Work

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

Year: 2018

Type: article

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 1 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. Although 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.

Source: Cellular Microbiology

DOI: 10.1111/cmi.12855

Authors: Xuran Zhuang, Xiuli Yang, Amanda S. Altieri, Daniel C. Nelson, Utpal Pal

Institutions: University of Maryland, College Park, National Institute of Standards and Technology, Institute for Bioscience and Biotechnology Research, Virginia–Maryland College of Veterinary Medicine

Language: English

Topic: Vector-borne infectious diseases

Subfield: Parasitology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: Global Lyme Alliance, National Institutes of Health, National Institute of Allergy and Infectious Diseases