Antibiotic Susceptibility and Molecular Characterization of Campylobacter jejuni Strain Isolated from a Guillain Barré Syndrome Child

Noreen, Zobia; Abrar, Mohammad; Siddiqui, Fariha; Faryal, Rani; Hamid, Muhammad Haroon; Bokhari, Habib

doi:10.1007/s12098-015-1923-z

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“…Campylobacter jejuni is one of the leading causes of bacterial-associated, food-borne gastroenteritis worldwide, and is responsible for more than 550 million cases per year [12]. Although the infection caused by C. jejuni is self-limiting, it can lead to serious complications, such as Guillain-Barr e syndrome and Miller Fisher syndrome [13][14][15]. As a food-borne pathogen, C. jejuni is transmitted predominantly via the consumption of contaminated poultry, milk, beef, pork, Abbreviations DLS, dynamic light scattering; DMSO, dimethyl sulfoxide; Hcp, hemolysin-coregulated protein; NCS, noncrystallographic symmetry; PBS, phosphate buffer saline; RBC, red blood cells; SRB, sulforhodamine B; T6SS, Type VI Secretion System.…”

Section: Introductionmentioning

confidence: 99%

“…Campylobacter jejuni is one of the leading causes of bacterial‐associated, food‐borne gastroenteritis worldwide, and is responsible for more than 550 million cases per year . Although the infection caused by C. jejuni is self‐limiting, it can lead to serious complications, such as Guillain–Barré syndrome and Miller Fisher syndrome . As a food‐borne pathogen, C. jejuni is transmitted predominantly via the consumption of contaminated poultry, milk, beef, pork, or water .…”

Section: Introductionmentioning

confidence: 99%

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Structural basis for the pathogenesis of Campylobacter jejuni Hcp1, a structural and effector protein of the Type VI Secretion System

et al. 2018

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The Type VI Secretion System (T6SS) provides enhanced virulence to Campylobacter jejuni and has been associated with a high incidence of bloody diarrhea. The hemolysin-coregulated protein (Hcp)-the hallmark of the T6SS-can act as a structural and effector protein. Unlike other T6SS-harboring bacteria, which possess multiple Hcp proteins each performing different functions, C. jejuni possesses only one Hcp protein, and its structural and functional role has not been elucidated previously. Here, we report the structure and functional studies of Hcp from C. jejuni. We found similarities between the hexameric ring structure of Hcp-Cj and that of Hcp3 from Pseudomonas aeruginosa. Through functional studies, we showed two roles for Hcp-Cj that is, in cytotoxicity toward HepG2 cells and in biofilm formation in C. jejuni. In structure-based mutational analyses, we showed that an Arg-to-Ala mutation at position 30 within the extended loop results in a significant decrease in cytotoxicity, suggesting a role for this loop in binding to the host cell. However, this mutation does not affect its biofilm formation function. Collectively, this study supports the dual role of Hcp-Cj as a structural and effector protein in C. jejuni.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%