PMID- 21900246
OWN - NLM
STAT- MEDLINE
DCOM- 20120116
LR  - 20220129
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 286
IP  - 47
DP  - 2011 Nov 25
TI  - Chemical structure of Trichomonas vaginalis surface lipoglycan: a role for short 
      galactose (beta1-4/3) N-acetylglucosamine repeats in host cell interaction.
PG  - 40494-508
LID - 10.1074/jbc.M111.280578 [doi]
AB  - The extracellular parasite Trichomonas vaginalis contains a surface 
      glycoconjugate that appears to mediate parasite-host cell interaction via binding 
      to human galectin-1. This glycoconjugate also elicits cytokine production from 
      human vaginal epithelial cells, implicating its role in modulation of host immune 
      responses. We have analyzed the structure of this glycoconjugate, previously 
      described to contain the sugars rhamnose (Rha), N-acetylglucosamine (GlcNAc), 
      galactose (Gal), xylose (Xyl), N-acetylgalactosamine (GalNAc), and glucose (Glc), 
      using gas chromatograph mass spectrometry (GC-MS), matrix-assisted laser 
      desorption/ionization time of flight mass spectrometry (MALDI-TOF), electrospray 
      MS/MS, and nuclear magnetic resonance (NMR), combined with chemical and enzymatic 
      digestions. Our data reveal a complex structure, named T. vaginalis lipoglycan 
      (TvLG), that differs markedly from Leishmania lipophosphoglycan and Entamoeba 
      lipopeptidophosphoglycan and is devoid of phosphosaccharide repeats. TvLG is 
      composed of an alpha1-3 linked polyrhamnose core, where Rha residues are substituted 
      at the 2-position with either beta-Xyl or chains of, on average, five 
      N-acetyllactosamine (-3Galbeta1-4GlcNAcbeta1-) (LacNAc) units and occasionally 
      lacto-N-biose (-3Galbeta1-3GlcNAcbeta1-) (LNB). These chains are themselves 
      periodically substituted at the Gal residues with Xyl-Rha. These structural 
      analyses led us to test the role of the poly-LacNAc/LNB chains in parasite 
      binding to host cells. We found that reduction of poly-LacNAc/LNB chains 
      decreased the ability of TvLG to compete parasite binding to host cells. In 
      summary, our data provide a new model for the structure of TvLG, composed of a 
      polyrhamnose backbone with branches of Xyl and poly-LacNAc/LNB. Furthermore, the 
      poly-LacNAc side chains are shown to be involved in parasite-host cell 
      interaction.
FAU - Ryan, Christopher M
AU  - Ryan CM
AD  - Department of Microbiology, Immunology, and Molecular Genetics, UCLA, Los 
      Angeles, California 90095-1489, USA.
FAU - Mehlert, Angela
AU  - Mehlert A
FAU - Richardson, Julia M
AU  - Richardson JM
FAU - Ferguson, Michael A J
AU  - Ferguson MA
FAU - Johnson, Patricia J
AU  - Johnson PJ
LA  - eng
GR  - 085622/Wellcome Trust/United Kingdom
GR  - G0500923/MRC_/Medical Research Council/United Kingdom
GR  - R01 AI069058/AI/NIAID NIH HHS/United States
GR  - 083481/WT_/Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20110907
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Lipopolysaccharides)
RN  - 50787-09-2 (galactosyl-1,3-N-acetylglucosamine)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
RN  - QN34XC755A (Rhamnose)
RN  - V956696549 (Acetylglucosamine)
SB  - IM
MH  - Acetylglucosamine/*analogs & derivatives/chemistry/metabolism
MH  - Carbohydrate Sequence
MH  - Cell Adhesion
MH  - *Cell Communication
MH  - Cell Line
MH  - Epithelial Cells/cytology
MH  - Female
MH  - Glycoside Hydrolases/metabolism
MH  - Humans
MH  - Hydrolysis
MH  - Lipopolysaccharides/*chemistry/*metabolism
MH  - Magnetic Resonance Spectroscopy
MH  - Mass Spectrometry
MH  - Methylation
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - *Repetitive Sequences, Nucleic Acid
MH  - Rhamnose/chemistry/metabolism
MH  - Trichomonas vaginalis/*metabolism
MH  - Vagina/cytology
PMC - PMC3220458
EDAT- 2011/09/09 06:00
MHDA- 2012/01/17 06:00
PMCR- 2011/09/07
CRDT- 2011/09/09 06:00
PHST- 2011/09/09 06:00 [entrez]
PHST- 2011/09/09 06:00 [pubmed]
PHST- 2012/01/17 06:00 [medline]
PHST- 2011/09/07 00:00 [pmc-release]
AID - S0021-9258(20)50399-2 [pii]
AID - M111.280578 [pii]
AID - 10.1074/jbc.M111.280578 [doi]
PST - ppublish
SO  - J Biol Chem. 2011 Nov 25;286(47):40494-508. doi: 10.1074/jbc.M111.280578. Epub 
      2011 Sep 7.