Document Detail

Identification of an ATPase, MsmK, which energizes multiple carbohydrate ABC transporters in Streptococcus pneumoniae.
MedLine Citation:
PMID:  21825065     Owner:  NLM     Status:  MEDLINE    
Streptococcus pneumoniae is the leading cause of community-acquired pneumonia and results in over 1 million deaths each year worldwide. Asymptomatic colonization of the airway precedes disease, and acquisition of carbohydrates from the host environment is necessary for bacterial survival. We previously demonstrated that S. pneumoniae cleaves sialic acid from human glycoconjugates to be used as a carbohydrate source. The satABC genes are required for growth and import of sialic acid. The satABC genes are predicted to encode components of an ABC transporter but not the ATPases essential to energize transport. As this subunit is essential, an ATPase must be encoded elsewhere in the genome. We identified msmK as a candidate based on similarity to other known carbohydrate ATPases. Recombinant MsmK hydrolyzed ATP, revealing that MsmK is an ATPase. An msmK mutant was reduced in growth on and transport of sialic acid, demonstrating that MsmK is the ATPase energizing the sialic acid transporter. In addition to satABC, S. pneumoniae contains five other loci that are predicted to encode CUT1 family carbohydrate ABC transporter components; each of these lacks a predicted ATPase. Data indicate that msmK is also required for growth on raffinose and maltotetraose, which are the substrates of two other characterized carbohydrate ABC transporters. Furthermore, an msmK mutant was reduced in airway colonization. Together, these data imply that in vivo, MsmK energizes multiple carbohydrate transporters in S. pneumoniae. This is the first demonstration of a shared ATPase in a pathogenic bacterium.
Carolyn Marion; Andrew E Aten; Shireen A Woodiga; Samantha J King
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-08-08
Journal Detail:
Title:  Infection and immunity     Volume:  79     ISSN:  1098-5522     ISO Abbreviation:  Infect. Immun.     Publication Date:  2011 Oct 
Date Detail:
Created Date:  2011-09-22     Completed Date:  2011-11-15     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4193-200     Citation Subset:  IM    
The Research Institute at Nationwide Children's Hospital, Center for Microbial Pathogenesis, Columbus, OH 43205-2696, USA.
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MeSH Terms
ATP-Binding Cassette Transporters / genetics,  metabolism*
Adenosine Triphosphatases / genetics,  metabolism*
Bacterial Proteins / genetics,  metabolism
Biological Transport*
Carbohydrate Metabolism*
Gene Expression Regulation, Bacterial
Maltose / analogs & derivatives,  metabolism
N-Acetylneuraminic Acid / metabolism
Organic Anion Transporters / genetics,  metabolism
Raffinose / metabolism
Streptococcus pneumoniae / enzymology*,  genetics,  metabolism
Symporters / genetics,  metabolism
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/Organic Anion Transporters; 0/Symporters; 0/sialic acid transport proteins; 131-48-6/N-Acetylneuraminic Acid; 34612-38-9/maltotetraose; 512-69-6/Raffinose; 69-79-4/Maltose; EC 3.6.1.-/Adenosine Triphosphatases

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

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