Work

Controlled Proteolysis of an Essential Virulence Determinant Dictates Infectivity of Lyme Disease Pathogens

Year: 2022

Type: article

Abstract: The Borrelia burgdorferi BB0323 protein undergoes a complex yet poorly defined proteolytic maturation event that generates N-terminal and C-terminal proteins with essential functions in cell growth and infection. Here, we report that a borrelial protease, B. burgdorferi high temperature requirement A protease (BbHtrA), cleaves BB0323 between asparagine (N) and leucine (L) at positions 236 and 237, while the replacement of these residues with alanine in the mutant protein prevents its cleavage, despite preserving its normal secondary structure.

Source: Infection and Immunity

DOI: 10.1128/iai.00059-22

Authors: Meghna Thakur, Sandhya Bista, Shelby D. Foor, Shraboni Dutta, Xiuli Yang, Michael Ronzetti, Vipin S. Rana, Chrysoula Kitsou, Sara B. Linden, Amanda S. Altieri, Bolormaa Baljinnyam, Daniel C. Nelson, Anton Simeonov, Utpal Pal

Institutions: University of Maryland, College Park, National Center for Advancing Translational Sciences, 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

Open Access status: green

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

Awards: BBA57-Mediated Borrelial Persistence, Genesis of Inflammation and Immunity, Borrelia gene products critical for natural infection cycle, Identification of inhibitors of BB323 and BB238 interaction in Borrelia burgdorferi (chronic Lyme disease), Ixodes scapularis Immuno-Developmental and Metabolic Signaling Pathways and Interference with Ticks and Tick-borne Pathogens

OpenAlex ID: W4223551454

FWCI: 0.993

Cites: 50

Cited by: 8

Related to: 10