Inhibition of Fibrinolysis by Streptococcal Phage Lysin SM1

Author:

Ji Hyun Jung12,Zhi Yong13,Lee Ji Hee1,Ahn Ki Bum1,Seo Ho Seong13ORCID,Sullam Paul M.4ORCID

Affiliation:

1. Research Division for Radiation Science, Korea Atomic Energy Research Institute, Jeongeup, Republic of Korea

2. Department of Oral Microbiology and Immunology, DRI, and BK21 Plus Program, School of Dentistry, Seoul National University, Seoul, Republic of Korea

3. Department of Radiation Science, University of Science and Technology, Daejeon, Republic of Korea

4. Department of Medicine, Veterans Affairs Medical Center and University of California, San Francisco, California, USA

Abstract

The interaction of streptococci with human fibrinogen and platelets on damaged endocardium is a central event in the pathogenesis of infective endocarditis. Streptococcus oralis can bind platelets via the interaction of bacteriophage lysin SM1 with fibrinogen on the platelet surface, and this process has been associated with increased virulence in an animal model of endocarditis. We now report that lysin SM1 binds to the αC region of the human fibrinogen Aα chain.

Funder

HHS | National Institutes of Health

National Research Foundation of Korea

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

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