Document Detail

Resistance of Mycoplasma pulmonis to complement lysis is dependent on the number of Vsa tandem repeats: shield hypothesis.
MedLine Citation:
PMID:  15557605     Owner:  NLM     Status:  MEDLINE    
The Vsa proteins are associated with the virulence of the murine respiratory pathogen Mycoplasma pulmonis. The antigens consist of a conserved N-terminal region that is combined with one of several different variable C-terminal regions comprised of tandem repeats. M. pulmonis strains that produce VsaA with about 40 tandem repeats do not adhere to polystyrene or erythrocytes and are highly resistant to complement killing. Strains that produce VsaA with three tandem repeats adhere strongly to polystyrene and erythrocytes and are highly susceptible to complement killing. We report here that the resistance to complement lysis was not due to a lack of activation of the complement cascade. Isolation and analysis of M. pulmonis strains that produced Vsa proteins other than VsaA (VsaG and VsaI) with either long or short repeat regions indicated that adherence to polystyrene and resistance to complement were dependent on the length of the repeat region but not on the Vsa type. Furthermore, M. pulmonis Vsa variants were susceptible to the polypeptide pore-forming molecule gramicidin D, independent of the Vsa type and length. Collectively, the data indicate the Vsa proteins nonspecifically mediate M. pulmonis surface interactions and function to sterically hinder access of complement to the mycoplasma cell membrane while permitting access of smaller molecules.
Warren L Simmons; Amy M Denison; Kevin Dybvig
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Infection and immunity     Volume:  72     ISSN:  0019-9567     ISO Abbreviation:  Infect. Immun.     Publication Date:  2004 Dec 
Date Detail:
Created Date:  2004-11-23     Completed Date:  2004-12-30     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6846-51     Citation Subset:  IM    
Department of Genetics, University of Alabama at Birmingham, 720 South 20th Street, Kaul Room 720, Birmingham, AL 35294-0024, USA.
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MeSH Terms
Antigens, Bacterial / chemistry,  genetics,  physiology*
Antigens, Surface / physiology
Bacterial Adhesion
Complement Activation*
Gramicidin / pharmacology
Guinea Pigs
Mycoplasma pulmonis / drug effects,  immunology*,  pathogenicity
Tandem Repeat Sequences*
Grant Support
Reg. No./Substance:
0/Antigens, Bacterial; 0/Antigens, Surface; 1405-97-6/Gramicidin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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