Investigation of pneumococcal virulence factors in the infection process
Author:
Affiliation:
1. Department of Oral and Molecular Microbiology, Osaka University Graduate School of Dentistry
Publisher
Japanese Society for Bacteriology
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/jsb/75/2/75_173/_pdf
Reference42 articles.
1. 1)Avery, O.T., Macleod, C.M., McCarty, M. (1944): Studies on the Chemical Nature of the Substance Inducing Transformation of Pneumococcal Types: Induction of Transformation by a Desoxyribonucleic Acid Fraction Isolated from Pneumococcus Type III. J. Exp. Med. 79, 137–158.
2. 2)Beiter, K., Wartha, F., Albiger, B., Normark, S., Zychlinsky, A., Henriques-Normark, B. (2006): An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps. Curr. Biol. 16, 401–407.
3. 3)Bek-Thomsen, M., Poulsen, K., Kilian, M. (2012): Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and related commensal species. mBio 3, e00303-12.
4. 4)Bergmann, S., Rohde, M., Chhatwal, G.S., Hammerschmidt, S. (2001): alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol. Microbiol. 40, 1273–1287.
5. 5)Beulin, D.S., Yamaguchi, M., Kawabata, S., Ponnuraj, K. (2014): Crystal structure of PfbA, a surface adhesin of Streptococcus pneumoniae, provides hints into its interaction with fibronectin. Int. J. Biol. Macromol. 64, 168–173.
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