Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/20088
Title: Leptospira interrogans enolase is secreted extracellularly and interacts with plasminogen
Authors: Nogueira, Sarah Veloso
Backstedt, Brian T
Smith, Alexis A
Qin, Jin-Hong
Wunder Junior, Elsio Augusto
Ko, Albert Icksang
Pal, Utpal
Affilliation: University of Maryland. Virginia Maryland Regional College of Veterinary Medicine. Department of Veterinary Medicine. Maryland, USA
University of Maryland. Virginia Maryland Regional College of Veterinary Medicine. Department of Veterinary Medicine. Maryland, USA
University of Maryland. Virginia Maryland Regional College of Veterinary Medicine. Department of Veterinary Medicine. Maryland, USA
University of Maryland. Virginia Maryland Regional College of Veterinary Medicine. Department of Veterinary Medicine. Maryland, USA
Yale University School of Public Health. Department of Epidemiology of Microbial Diseases. New Haven, Connecticut, USA
Yale University School of Public Health. Department of Epidemiology of Microbial Diseases. New Haven, Connecticut, USA
University of Maryland. Virginia Maryland Regional College of Veterinary Medicine. Department of Veterinary Medicine. Maryland, USA
Abstract: Leptospira interrogans is the agent for leptospirosis, an important zoonosis in humans and animals across the globe. Surface proteins of invading pathogens, such as L. interrogans, are thought to be responsible for successful microbial persistence in vivo via interaction with specific host components. In particular, a number of invasive infectious agents exploit host proteolytic pathways, such as one involving plasminogen (Pg), which aid in efficient pathogen dissemination within the host. Here we show that L. interrogans serovar Lai binds host Pg and that the leptospiral gene product LA1951, annotated as enolase, is involved in this interaction. Interestingly, unlike in related pathogenic Spirochetes, such as Borrelia burgdorferi, LA1951 is not readily detectable in the L. interrogans outer membrane. We show that the antigen is indeed secreted extracellularly; however, it can reassociate with the pathogen surface, where it displays Pg-binding and measurable enzymatic activity. Hamsters infected with L. interrogans also develop readily detectable antibody responses against enolase. Taken together, our results suggest that the L. interrogans enolase has evolved to play a role in pathogen interaction with host molecules, which may contribute to the pathogenesis of leptospirosis.
Keywords: Leptospira interrogans
Bacterial Proteins
Plasminogen
Cricetinae
Animals
keywords: Leptospira interrogans
Proteínas
Plasminogenio
Cricetinae
Animais
Issue Date: 2013
Publisher: Public Library of Science
Citation: NOGUEIRA, S. V. et al. Leptospira interrogans enolase is secreted extracellularly and interacts with plasminogen. PLoS One, v. 8, n. 10, p. e78150, 2013.
Description: Ko, Albert Icksang “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.
DOI: 10.1371/journal.pone.0078150
ISSN: 1932-6203
Copyright: open access
Appears in Collections:IGM - Artigos de Periódicos

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