PMID- 22556361
OWN - NLM
STAT- MEDLINE
DCOM- 20121130
LR  - 20200826
IS  - 1465-2080 (Electronic)
IS  - 1350-0872 (Linking)
VI  - 158
IP  - Pt 8
DP  - 2012 Aug
TI  - The VC1777-VC1779 proteins are members of a sialic acid-specific subfamily of 
      TRAP transporters (SiaPQM) and constitute the sole route of sialic acid uptake in 
      the human pathogen Vibrio cholerae.
PG  - 2158-2167
LID - 10.1099/mic.0.059659-0 [doi]
AB  - Sialic acids are nine-carbon amino sugars that are present on all mucous 
      membranes and are often used by bacteria as nutrients. In pathogenic Vibrio the 
      genes for sialic acid catabolism (SAC) are known to be important for host 
      colonization, yet the route for sialic acid uptake is not proven. Vibrio cholerae 
      contains a tripartite ATP-independent periplasmic (TRAP) transporter, SiaPQM 
      (VC1777-VC1779), encoded by genes within the Vibrio pathogenicity island-2 
      (VPI-2), which are adjacent to the SAC genes nanA, nanE and nanK. We demonstrate 
      a correlation of the occurrence of VPI-2 and the ability of Vibrio to grow on the 
      common sialic acid N-acetylneuraminic acid (Neu5Ac), and that a V. cholerae 
      N16961 mutant defective in vc1777, encoding the large membrane protein component 
      of the TRAP transporter, SiaM, is unable to grow on Neu5Ac as the sole carbon 
      source. Using the genome context and known structures of the SiaP protein 
      component of the TRAP transporter, we define a subfamily of Neu5Ac-specific TRAP 
      transporters, of which the vc1777-vc1779 genes are the only representatives in V. 
      cholerae. A recent report has suggested that an entirely different TRAP 
      transporter (VC1927-VC1929) is the Neu5Ac transporter in V. cholerae. 
      Bioinformatics and genomic analysis suggest strongly that this is a 
      C(4)-dicarboxylate-specific TRAP transporter, and indeed disruption of vc1929 
      results in a defect in growth on C(4)-dicarboxylates but not Neu5Ac. Together 
      these data demonstrate unequivocally that the siaPQM-encoded TRAP transporter 
      within VPI-2 is the sole sialic acid transporter in V. cholerae.
FAU - Chowdhury, Nityananda
AU  - Chowdhury N
AD  - Department of Biological Sciences, University of Delaware, Newark, DE 19716, USA.
FAU - Norris, Jessica
AU  - Norris J
AD  - Department of Biology (Area 10), University of York, York YO10 5YW, UK.
FAU - McAlister, Erin
AU  - McAlister E
AD  - Department of Biology (Area 10), University of York, York YO10 5YW, UK.
FAU - Lau, S Y Kathy
AU  - Lau SYK
AD  - Department of Biology (Area 10), University of York, York YO10 5YW, UK.
FAU - Thomas, Gavin H
AU  - Thomas GH
AD  - Department of Biology (Area 10), University of York, York YO10 5YW, UK.
FAU - Boyd, E Fidelma
AU  - Boyd EF
AD  - Department of Biological Sciences, University of Delaware, Newark, DE 19716, USA.
LA  - eng
GR  - BB/F014759/1/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20120503
PL  - England
TA  - Microbiology (Reading)
JT  - Microbiology (Reading, England)
JID - 9430468
RN  - 0 (Bacterial Proteins)
RN  - 0 (Membrane Transport Proteins)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/genetics/*metabolism
MH  - Biological Transport
MH  - Cholera/*microbiology
MH  - Humans
MH  - Membrane Transport Proteins/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - N-Acetylneuraminic Acid/*metabolism
MH  - Phylogeny
MH  - Vibrio cholerae/classification/genetics/*metabolism
EDAT- 2012/05/05 06:00
MHDA- 2012/12/10 06:00
CRDT- 2012/05/05 06:00
PHST- 2012/05/05 06:00 [entrez]
PHST- 2012/05/05 06:00 [pubmed]
PHST- 2012/12/10 06:00 [medline]
AID - 10.1099/mic.0.059659-0 [doi]
PST - ppublish
SO  - Microbiology (Reading). 2012 Aug;158(Pt 8):2158-2167. doi: 
      10.1099/mic.0.059659-0. Epub 2012 May 3.