PMID- 19749047
OWN - NLM
STAT- MEDLINE
DCOM- 20091117
LR  - 20211020
IS  - 1098-5530 (Electronic)
IS  - 0021-9193 (Print)
IS  - 0021-9193 (Linking)
VI  - 191
IP  - 22
DP  - 2009 Nov
TI  - Functional characterization of flagellin glycosylation in Campylobacter jejuni 
      81-176.
PG  - 7086-93
LID - 10.1128/JB.00378-09 [doi]
AB  - The major flagellin of Campylobacter jejuni strain 81-176, FlaA, has been shown 
      to be glycosylated at 19 serine or threonine sites, and this glycosylation is 
      required for flagellar filament formation. Some enzymatic components of the 
      glycosylation machinery of C. jejuni 81-176 are localized to the poles of the 
      cell in an FlhF-independent manner. Flagellin glycosylation could be detected in 
      flagellar mutants at multiple levels of the regulatory hierarchy, indicating that 
      glycosylation occurs independently of the flagellar regulon. Mutants were 
      constructed in which each of the 19 serine or threonines that are glycosylated in 
      FlaA was converted to an alanine. Eleven of the 19 mutants displayed no 
      observable phenotype, but the remaining 8 mutants had two distinct phenotypes. 
      Five mutants (mutations S417A, S436A, S440A, S457A, and T481A) were fully motile 
      but defective in autoagglutination (AAG). Three other mutants (mutations S425A, 
      S454A, and S460A) were reduced in motility and synthesized truncated flagellar 
      filaments. The data implicate certain glycans in mediating filament-filament 
      interactions resulting in AAG and other glycans appear to be critical for 
      structural subunit-subunit interactions within the filament.
FAU - Ewing, Cheryl P
AU  - Ewing CP
AD  - Enteric Diseases Department, Naval Medical Research Center, 503 Robert Grant 
      Ave., Silver Spring, MD 20910, USA.
FAU - Andreishcheva, Ekaterina
AU  - Andreishcheva E
FAU - Guerry, Patricia
AU  - Guerry P
LA  - eng
GR  - R01 AI043559/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20090911
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Bacterial Proteins)
RN  - 12777-81-0 (Flagellin)
RN  - 133606-66-3 (flaA protein, bacteria)
SB  - IM
MH  - Bacterial Proteins/chemistry/genetics/metabolism
MH  - Campylobacter jejuni/genetics/*metabolism/ultrastructure
MH  - Flagella/genetics/metabolism/ultrastructure
MH  - Flagellin/chemistry/genetics/*metabolism
MH  - Glycosylation
MH  - Immunoblotting
MH  - Microscopy, Electron, Transmission
MH  - Mutagenesis, Site-Directed
PMC - PMC2772469
EDAT- 2009/09/15 06:00
MHDA- 2009/11/18 06:00
PMCR- 2010/05/01
CRDT- 2009/09/15 06:00
PHST- 2009/09/15 06:00 [entrez]
PHST- 2009/09/15 06:00 [pubmed]
PHST- 2009/11/18 06:00 [medline]
PHST- 2010/05/01 00:00 [pmc-release]
AID - JB.00378-09 [pii]
AID - 0378-09 [pii]
AID - 10.1128/JB.00378-09 [doi]
PST - ppublish
SO  - J Bacteriol. 2009 Nov;191(22):7086-93. doi: 10.1128/JB.00378-09. Epub 2009 Sep 
      11.