Streptococcus mutans Surface α-Enolase Binds Salivary Mucin MG2 and Human Plasminogen-Reference-Cited by-同舟云学术

Streptococcus mutans Surface α-Enolase Binds Salivary Mucin MG2 and Human Plasminogen

Published:2004-11 Issue:11 Volume:72 Page:6748-6752
ISSN:0019-9567
Container-title:Infection and Immunity
language:en
Short-container-title:Infect Immun

Author:

Ge Jingping¹,Catt Diana M.²,Gregory Richard L.¹²

Affiliation:

1. Department of Pathology and Laboratory Medicine, School of Medicine

2. Department of Oral Biology, School of Dentistry, Indiana University, Indianapolis, Indiana

Abstract

ABSTRACT Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis identified enolase as a cell surface component of Streptococcus mutans , which was confirmed by enzyme-linked immunosorbent assay, Western blotting, and transmission electron microscopy. Surface enolase was demonstrated to bind to human plasminogen and salivary mucin MG2. The results suggested a role for enolase in S. mutans attachment, clearance, or breach of the bloodstream barrier.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Link

https://journals.asm.org/doi/pdf/10.1128/IAI.72.11.6748-6752.2004

Reference34 articles.

1. Ajdic, D., W. M. McShan, R. E. McLaughlin, G. Savic, J. Chang, M. B. Carson, C. Primeaux, R. Tian, S. Kenton, H. Jia, S. Lin, Y. Qian, S. Li, H. Zhu, F. Najar, H. Lai, J. White, B. A. Joe, and J. J. Ferretti. 2002. Genomic sequence of Streptococcus mutans UA159, a cariogenic dental pathogen. Proc. Natl. Acad. Sci. USA99:14434-14439.

2. Banas, A. J. 2004. Virulence properties of Streptococcus mutans. Front. Biosci.9:1267-1277.

3. Bergmann, S., M. Rohde, G. S. Chhatwal, and S. Hammerschmidt. 2001. α-Enolase of Streptococcus pneumoniae is a plasminogen-binding protein displayed on the bacterial cell surface. Mol. Microbiol.40:1273-1287.

4. Interaction of a salivary mucin-secretory immunoglobulin A complex with mucosal pathogens

5. Bottalico, L. A., N. C. Kendrick, A. Keller, Y. Li, and I. Tabas. 1993. Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in expression or modification of specific cellular proteins, including increase in an α-enolase isoform. Arterioscl. Thromb.13:264-275.

Cited by 83 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Transient bacteremia following the removal of four different types of rapid palatal expanders;Journal of Orofacial Orthopedics / Fortschritte der Kieferorthopädie;2024-03-25

2. Unveiling the functional significance of the 14.3.3 protein: A key player in Paracoccidioides brasiliensis biofilm formation;Microbial Pathogenesis;2024-03

3. Mycobacterium tuberculosis H37Rv enolase (Rv1023)- expression, characterization and effect of host dependent modifications on protein functionality;Biochimie;2023-11

4. Moonlighting proteins [ML proteins]: The pandora's box of insidious oro-dental diseases;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2023-04

5. Virulence factors of Streptococcus anginosus – a molecular perspective;Frontiers in Microbiology;2022-10-26