scholarly journals Crystal structure of virulence factor CJ0248 from Campylobacter jejuni at 2.25 Å resolution reveals a new fold

2005 ◽  
Vol 62 (1) ◽  
pp. 292-296 ◽  
Author(s):  
Qingping Xu ◽  
Robert Schwarzenbacher ◽  
Daniel McMullan ◽  
Polat Abdubek ◽  
Sanjay Agarwalla ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Campylobacter Jejuni ◽  
Virulence Factor

scholarly journals Multi-Omics Approach Reveals the Potential Core Vaccine Targets for the Emerging Foodborne Pathogen Campylobacter jejuni

2021 ◽  
Vol 12 ◽  
Author(s):  
Hengchun Cao ◽  
Hanxiao Xu ◽  
Chunhui Ning ◽  
Li Xiang ◽  
Qiufang Ren ◽  
...  
Keyword(s):  
Campylobacter Jejuni ◽  
Virulence Factor ◽  
Target Genes ◽  
Bacterial Resistance ◽  
Animal Experiments ◽  
Foodborne Pathogen ◽  
Gene Families ◽  
Intestinal Loop ◽  
Potential Core ◽  
New Vaccines

Campylobacter jejuni is a leading cause of bacterial gastroenteritis in humans around the world. The emergence of bacterial resistance is becoming more serious; therefore, development of new vaccines is considered to be an alternative strategy against drug-resistant pathogen. In this study, we investigated the pangenome of 173 C. jejuni strains and analyzed the phylogenesis and the virulence factor genes. In order to acquire a high-quality pangenome, genomic relatedness was firstly performed with average nucleotide identity (ANI) analyses, and an open pangenome of 8,041 gene families was obtained with the correct taxonomy genomes. Subsequently, the virulence property of the core genome was analyzed and 145 core virulence factor (VF) genes were obtained. Upon functional genomics and immunological analyses, five core VF proteins with high antigenicity were selected as potential core vaccine targets for humans. Furthermore, functional annotations indicated that these proteins are involved in important molecular functions and biological processes, such as adhesion, regulation, and secretion. In addition, transcriptome analysis in human cells and pig intestinal loop proved that these vaccine target genes are important in the virulence of C. jejuni in different hosts. Comprehensive pangenome and relevant animal experiments will facilitate discovering the potential core vaccine targets with improved efficiency in reverse vaccinology. Likewise, this study provided some insights into the genetic polymorphism and phylogeny of C. jejuni and discovered potential vaccine candidates for humans. Prospective development of new vaccines using the targets will be an alternative to the use of antibiotics and prevent the development of multidrug-resistant C. jejuni in humans and even other animals.

The structure of urease inactivated by Ag(i): a new paradigm for enzyme inhibition by heavy metals

2018 ◽  
Vol 47 (25) ◽  
pp. 8240-8247 ◽  
Author(s):  
Luca Mazzei ◽  
Michele Cianci ◽  
Antonio Gonzalez Vara ◽  
Stefano Ciurli
Keyword(s):  
Crystal Structure ◽  
Heavy Metals ◽  
Enzyme Inhibition ◽  
Virulence Factor ◽  
Soil Nitrogen ◽  
Nitrogen Fertilization ◽  
Enzyme Complex ◽  
Human Pathogens ◽  
New Paradigm

The molecular details of the inactivation of urease, a nickel-dependent virulence factor for human pathogens and negatively affecting the efficiency of soil nitrogen fertilization, are elucidated through the crystal structure of the enzyme complex with Ag(i).

scholarly journals CapC, a Novel Autotransporter and Virulence Factor ofCampylobacter jejuni

2018 ◽  
Vol 84 (16) ◽  
Author(s):  
Jai W. Mehat ◽  
Simon F. Park ◽  
Arnoud H. M. van Vliet ◽  
Roberto M. La Ragione
Keyword(s):  
Public Health ◽  
Epithelial Cells ◽  
Campylobacter Jejuni ◽  
Virulence Factor ◽  
Causative Agent ◽  
Galleria Mellonella ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Content Type ◽  
Reduced Adherence

ABSTRACTCampylobacter jejuniis recognized as an important causative agent of bacterial gastroenteritis in the developed world. Despite the identification of several factors contributing to infection, characterization of the virulence strategies employed byC. jejuniremains a significant challenge. Bacterial autotransporter proteins are a major class of secretory proteins in Gram-negative bacteria, and notably, many autotransporter proteins contribute to bacterial virulence. The aim of this study was to characterize theC. jejuni81116 C8J_1278 gene (capC), predicted to encode an autotransporter protein, and examine the contribution of this factor to virulence ofC. jejuni. The predicted CapC protein has a number of features that are consistent with autotransporters, including the N-terminal signal sequence and the C-terminal β-barrel domain and was determined to localize to the outer membrane. Inactivation of thecapCgene inC. jejuni81116 andC. jejuniM1 resulted in reduced insecticidal activity inGalleria mellonellalarvae. Furthermore,C. jejuni capCmutants displayed significantly reduced adherence to and invasion of nonpolarized, partially differentiated Caco-2 and T84 intestinal epithelial cells. Gentamicin treatment showed that the reduced invasion of thecapCmutant is primarily caused by reduced adherence to intestinal epithelial cells, not by reduced invasion capability.C. jejuni capCmutants caused reduced interleukin 8 (IL-8) secretion from intestinal epithelial cells and elicited a significantly diminished immune reaction inGallerialarvae, indicating that CapC functions as an immunogen. In conclusion, CapC is a new virulence determinant ofC. jejunithat contributes to the integral infection process of adhesion to human intestinal epithelial cells.IMPORTANCECampylobacter jejuniis a major causative agent of human gastroenteritis, making this zoonotic pathogen of significant importance to human and veterinary public health worldwide. The mechanisms by whichC. jejuniinteracts with intestinal epithelial cells and causes disease are still poorly understood due, in part, to the heterogeneity ofC. jejuniinfection biology. Given the importance ofC. jejunito public health, the need to characterize novel and existing virulence mechanisms is apparent. The significance of our research is in demonstrating the role of CapC, a novel virulence factor inC. jejunithat contributes to adhesion and invasion of the intestinal epithelium, thereby in part, addressing the dearth of knowledge concerning the factors involved inCampylobacterpathogenesis and the variation observed in the severity of human infection.

scholarly journals Crystal Structure of Phosphorylcholine Esterase Domain of the Virulence Factor Choline-binding Protein E fromStreptococcus pneumoniae

2005 ◽  
Vol 280 (31) ◽  
pp. 28591-28600 ◽  
Author(s):  
Gianpiero Garau ◽  
David Lemaire ◽  
Thierry Vernet ◽  
Otto Dideberg ◽  
Anne Marie Di Guilmi
Keyword(s):  
Crystal Structure ◽  
Virulence Factor ◽  
Binding Protein

scholarly journals Crystal Structure ofLeishmania majorOligopeptidase B Gives Insight into the Enzymatic Properties of a Trypanosomatid Virulence Factor

2010 ◽  
Vol 285 (50) ◽  
pp. 39249-39259 ◽  
Author(s):  
Karen McLuskey ◽  
Neil G. Paterson ◽  
Nicholas D. Bland ◽  
Neil W. Isaacs ◽  
Jeremy C. Mottram
Keyword(s):  
Crystal Structure ◽  
Virulence Factor ◽  
Enzymatic Properties ◽  
Insight Into

scholarly journals Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine protease

2000 ◽  
Vol 97 (5) ◽  
pp. 2235-2240 ◽  
Author(s):  
T. F. Kagawa ◽  
J. C. Cooney ◽  
H. M. Baker ◽  
S. McSweeney ◽  
M. Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Virulence Factor ◽  
Cysteine Protease ◽  
Group A Streptococcus ◽  
Group A

scholarly journals The crystal structure of the estA protein, a virulence factor from Streptococcus pneumoniae

2007 ◽  
Vol 70 (2) ◽  
pp. 578-583 ◽  
Author(s):  
Myung Hee Kim ◽  
Beom Sik Kang ◽  
Sujin Kim ◽  
Kyung-Jin Kim ◽  
Choong Hwan Lee ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptococcus Pneumoniae ◽  
Virulence Factor ◽  
Protein A
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