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Journal of Bacteriology, December 2001, p. 7387-7391, Vol. 183, No. 24
Department of Microbiology, University of
Georgia, Athens, Georgia 30602
Received 19 June 2001/Accepted 21 September 2001
The surface protein P65 is a constituent of the Mycoplasma
pneumoniae cytoskeleton and is present at reduced levels in
mutants lacking the cytadherence accessory protein HMW2. Pulse-chase
studies demonstrated that P65 is subject to accelerated turnover in the absence of HMW2. P65 was also less abundant in noncytadhering mutants
lacking HMW1 or P30 but was present at wild-type levels in mutants
lacking proteins A, B, C, and P1. P65 exhibited a polar localization
like that in wild-type M. pneumoniae in all mutants having normal levels of HMW1 and HMW2. Partial or complete loss of
these proteins, however, correlated with severe reduction in the P65
level and the inability to localize P65 properly.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.24.7387-7891.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Stability and Subcellular Localization of
Cytadherence-Associated Protein P65 in Mycoplasma
pneumoniae

*
Corresponding author. Mailing address: Department of
Microbiology, 523 Biological Sciences Bldg., University of Georgia,
Athens, GA 30602. Phone: (706) 542-2671. Fax: (706) 542-2674. E-mail: dkrause{at}arches.uga.edu.
Present address: Foodborne and Diarrheal Diseases Laboratory
Section, Centers for Disease Control and Prevention, 1600 Clifton Road,
NE, Atlanta, GA 30333.
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