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J. Biol. Chem., Vol. 276, Issue 51, 47966-47974, December 21, 2001
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From the Department of Microbiology, University of Alabama,
Birmingham, Alabama 35294
Tyrosine phosphorylation is associated with
polysaccharide synthesis in a number of Gram-positive and Gram-negative
bacteria. In Streptococcus pneumoniae, CpsB, CpsC, and CpsD
affect tyrosine phosphorylation and are critical for the production of
a mature capsule in vitro. To characterize the interactions
between these proteins and the phosphorylation event they modulate,
cps2B, cps2C, and cps2D from the
capsule type 2 S. pneumoniae D39 were cloned and expressed
both individually and in combination in Escherichia coli.
Cps2D purified from E. coli was not phosphorylated unless it was co-expressed with its cognate transmembrane domain, Cps2C. Purified phosphorylated Cps2D had tyrosine kinase activity and could phosphorylate both dephosphorylated Cps2D and an exogenous substrate (poly-Glu-Tyr) in the absence of ATP. Cps2B exhibited phosphatase activity against both purified phosphorylated Cps2D and p-nitrophenyl phosphate. An additional role for Cps2B
as an inhibitor of Cps2D phosphorylation was demonstrated in both
co-expression experiments in E. coli and in
vitro experiments where it blocked the transphosphorylation of
Cps2D even in the presence of the phosphatase inhibitor sodium
orthovanadate. cps2C and cps2D deletion mutants
in S. pneumoniae produced no detectable mature capsule during laboratory culture. Both were avirulent in systemic mouse infections and were unable to colonize the nasopharynx, suggesting that
the failure to produce capsule was not dependent on the environment. Based on these results, we propose a model for capsule regulation where
CpsB, CpsC, CpsD, and ATP form a stable complex that enhances capsule synthesis.
CpsB Is a Modulator of Capsule-associated Tyrosine Kinase
Activity in Streptococcus pneumoniae*
*
This work was supported by Public Health Service Grants
GM53017, AI28457, T32 GM08111, and T32 HL07553 from the National
Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Microbiology,
BBRB 661/12, 845 19th St. South, Birmingham, AL 35294. Tel.: 205-934-9531; Fax: 205-975-6715; E-mail:
jyother@uab.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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