{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T19:58:42Z","timestamp":1791316722359,"version":"4.3.1"},"reference-count":50,"publisher":"American Society for Microbiology","issue":"18","license":[{"start":{"date-parts":[[2014,9,15]],"date-time":"2014-09-15T00:00:00Z","timestamp":1410739200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2014,9,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Teichoic acid (TA), together with peptidoglycan (PG), represents a highly complex glycopolymer that ensures cell wall integrity and has several crucial physiological activities. Through an insertion-deletion mutation strategy, we show that \u0394\n            <jats:italic>rafX<\/jats:italic>\n            mutants are impaired in cell wall covalently attached TA (WTA)-PG biosynthesis, as evidenced by their abnormal banding patterns and reduced amounts of WTA in comparison with wild-type strains. Site-directed mutagenesis revealed an essential role for external loop 4 and some highly conserved amino acid residues in the function of RafX protein. The\n            <jats:italic>rafX<\/jats:italic>\n            gene was highly conserved in closely related streptococcal species, suggesting an important physiological function in the lifestyle of streptococci. Moreover, a strain D39 \u0394\n            <jats:italic>rafX<\/jats:italic>\n            mutant was impaired in bacterial growth, autolysis, bacterial division, and morphology. We observed that a strain R6 \u0394\n            <jats:italic>rafX<\/jats:italic>\n            mutant was reduced in adhesion relative to the wild-type R6 strain, which was supported by an inhibition assay and a reduced amount of CbpA protein on the \u0394\n            <jats:italic>rafX<\/jats:italic>\n            mutant bacterial cell surface, as shown by flow cytometric analysis. Finally, \u0394\n            <jats:italic>rafX<\/jats:italic>\n            mutants were significantly attenuated in virulence in a murine sepsis model. Together, these findings suggest that RafX contributes to the biosynthesis of WTA, which is essential for full pneumococcal virulence.\n          <\/jats:p>","DOI":"10.1128\/jb.01696-14","type":"journal-article","created":{"date-parts":[[2014,7,8]],"date-time":"2014-07-08T03:49:32Z","timestamp":1404791372000},"page":"3324-3334","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["A Novel Protein, RafX, Is Important for Common Cell Wall Polysaccharide Biosynthesis in Streptococcus pneumoniae: Implications for Bacterial Virulence"],"prefix":"10.1128","volume":"196","author":[{"given":"Kaifeng","family":"Wu","sequence":"first","affiliation":[{"name":"Key Laboratory of Diagnostic Medicine (Ministry of Education), College of Laboratory Medicine, Chongqing Medical University, Chongqing, 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