Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism

. 2010 Apr 05 ; 9 (4) : 1995-2005.

Jazyk angličtina Země Spojené státy americké Médium print

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid20175567

Grantová podpora
P41 RR018942-02 NCRR NIH HHS - United States
P41 RR018942-03S1 NCRR NIH HHS - United States
P41 RR018942-01A2 NCRR NIH HHS - United States
P41 RR018942-03 NCRR NIH HHS - United States
P41 RR018942 NCRR NIH HHS - United States

It appears that most glycoproteins found in pathogenic bacteria are associated with virulence. Despite the recent identification of novel virulence factors, the mechanisms of virulence in Francisella tularensis are poorly understood. In spite of its importance, questions about glycosylation of proteins in this bacterium and its potential connection with bacterial virulence have not been answered yet. In the present study, several putative Francisella tularensis glycoproteins were characterized through the combination of carbohydrate-specific detection and lectin affinity with highly sensitive mass spectrometry utilizing the bottom-up proteomic approach. The protein PilA that was recently found as being possibly glycosylated, as well as other proteins with designation as novel factors of virulence, were among the proteins identified in this study. The reported data compile the list of potential glycoproteins that may serve as a takeoff platform for a further definition of proteins modified by glycans, faciliting a better understanding of the function of protein glycosylation in pathogenicity of Francisella tularensis.

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