scholarly journals Yersinia outer-membrane protein B (YopB): a tool for identification of Yersinia pestis isolates

2006 ◽  
Vol 55 (4) ◽  
pp. 467-469 ◽  
Author(s):  
Rekha Khushiramani ◽  
Jyoti Shukla ◽  
Urmil Tuteja ◽  
Harsh Vardhan Batra
Keyword(s):  
Membrane Protein ◽  
Yersinia Pestis ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein B

scholarly journals Serological Reactivity and Biochemical Characterization of Methylated and Unmethylated Forms of a Recombinant Protein Fragment Derived from Outer Membrane Protein B of Rickettsia typhi

2008 ◽  
Vol 15 (4) ◽  
pp. 684-690 ◽  
Author(s):  
Chien-Chung Chao ◽  
Zhiwen Zhang ◽  
Hui Wang ◽  
Abdulnaser Alkhalil ◽  
Wei-Mei Ching
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Mass Spectrometry Analysis ◽  
Enzyme Linked Immunosorbent Assay ◽  
Composition Analysis ◽  
Rickettsia Typhi ◽  
Serological Reactivity ◽  
Lysine Residues ◽  
Protein B

ABSTRACT Rickettsia typhi, an obligate intracellular bacterium that causes murine typhus, possesses a heavily methylated outer membrane protein B (OmpB) antigen. This immunodominant antigen is responsible for serological reactions and is capable of eliciting protective immune responses with a guinea pig model. Western blot analysis of partially digested OmpB with patient sera revealed that most of the reactive fragments are larger than 20 kDa. One of these fragments, which is located at the N terminus (amino acids 33 to 273), fragment A (At), has been expressed in Escherichia coli. The expressed protein (rAt) was purified by chromatography and properly refolded by sequential dialysis. The refolded rAt protein was recognized by at least 87% of the typhus group patient sera as determined by enzyme-linked immunosorbent assay (ELISA). However, the titers were lower than those obtained with OmpB of R. typhi. Since native OmpB is hypermethylated at lysine residues, we chemically methylated the lysine residues in rAt. The methylation was confirmed by amino acid composition analysis, and the methylation pattern of the methylated rAt (mrAt) protein was similar to that of native At from OmpB, as revealed by liquid chromatography-mass spectrometry analysis. Both rAt and mrAt were evaluated in an ELISA for their serological reactivity with patient sera. Among patient sera tested, 83% exhibited higher titers with mrAt than with rAt. These results suggest that rAt, with or without methylation, can potentially replace rickettsia-derived OmpB or whole-cell antigen for the diagnosis of R. typhi infection.

scholarly journals Structure and Activity of the Outer Membrane Protein Ail from Yersinia Pestis

2015 ◽  
Vol 108 (2) ◽  
pp. 247a
Author(s):  
Yi Ding ◽  
Lynn M. Fujimoto ◽  
Yong Yao ◽  
Gregory V. Plano ◽  
Francesca M. Marassi
Keyword(s):  
Membrane Protein ◽  
Yersinia Pestis ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Structure And Activity

scholarly journals High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes

2017 ◽  
Vol 67 (3) ◽  
pp. 179-190 ◽  
Author(s):  
Yong Yao ◽  
Samit Kumar Dutta ◽  
Sang Ho Park ◽  
Ratan Rai ◽  
L. Miya Fujimoto ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
High Resolution ◽  
Membrane Protein ◽  
Yersinia Pestis ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Lipid Membranes ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy

scholarly journals Rickettsial outer-membrane protein B (rOmpB) mediates bacterial invasion through Ku70 in an actin, c-Cbl, clathrin and caveolin 2-dependent manner

2009 ◽  
Vol 11 (4) ◽  
pp. 629-644 ◽  
Author(s):  
Yvonne G. Y. Chan ◽  
Marissa M. Cardwell ◽  
Timothy M. Hermanas ◽  
Tsuneo Uchiyama ◽  
Juan J. Martinez
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Bacterial Invasion ◽  
Dependent Manner ◽  
Protein B
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