scholarly journals A σ28-Regulated Nonflagella Gene Contributes to Virulence of Campylobacter jejuni 81-176

2006 ◽  
Vol 74 (1) ◽  
pp. 769-772 ◽  
Author(s):  
Scarlett Goon ◽  
Cheryl P. Ewing ◽  
Maria Lorenzo ◽  
Dawn Pattarini ◽  
Gary Majam ◽  
...  

ABSTRACT A Campylobacter jejuni 81-176 mutant in Cj0977 was fully motile but reduced >3 logs compared to the parent in invasion of intestinal epithelial cells in vitro. The mutant was also attenuated in a ferret diarrheal disease model. Expression of Cj0977 protein was dependent on a minimal flagella structure.

2018 ◽  
Vol 149 ◽  
pp. 67-72 ◽  
Author(s):  
Ramila Cristiane Rodrigues ◽  
Anne-Lise Pocheron ◽  
Jean-Michel Cappelier ◽  
Odile Tresse ◽  
Nabila Haddad

2004 ◽  
Vol 72 (4) ◽  
pp. 2452-2455 ◽  
Author(s):  
Margaret I. Kanipes ◽  
Lindsay C. Holder ◽  
Adrian T. Corcoran ◽  
Anthony P. Moran ◽  
Patricia Guerry

ABSTRACT A waaF mutant of Campylobacter jejuni 81-176 showed decreased invasion of INT407 cells in vitro and increased sensitivity to some antibiotics compared to what was seen with the wild-type strain.


Microbiology ◽  
2007 ◽  
Vol 153 (2) ◽  
pp. 561-569 ◽  
Author(s):  
Catherine M. Byrne ◽  
Marguerite. Clyne ◽  
Billy. Bourke

2012 ◽  
Vol 80 (7) ◽  
pp. 2361-2370 ◽  
Author(s):  
Muhammad Afzal Javed ◽  
Shaun A. Cawthraw ◽  
Abiyad Baig ◽  
Jianjun Li ◽  
Alan McNally ◽  
...  

ABSTRACTCampylobacter jejuniis a major cause of bacterial food-borne enteritis worldwide, and invasion into intestinal epithelial cells is an important virulence mechanism. Recently we reported the identification of hyperinvasiveC. jejunistrains and created a number of transposon mutants of one of these strains, some of which exhibited reduced invasion into INT-407 and Caco-2 cells. In one such mutant the transposon had inserted into a homologue ofcj1136, which encodes a putative galactosyltransferase according to the annotation of theC. jejuniNCTC11168 genome. In the current study, we investigated the role ofcj1136inC. jejunivirulence, lipooligosaccharide (LOS) biosynthesis, and host colonization by targeted mutagenesis and complementation of the mutation. Thecj1136mutant showed a significant reduction in invasion into human intestinal epithelial cells compared to the wild-type strain 01/51. Invasion levels were partially restored on complementing the mutation. The inactivation ofcj1136resulted in the production of truncated LOS, while biosynthesis of a full-length LOS molecule was restored in the complemented strain. Thecj1136mutant showed an increase in sensitivity to the bile salts sodium taurocholate and sodium deoxycholate and significantly increased sensitivity to polymyxin B compared to the parental strain. Importantly, the ability of the mutant to colonize 1-day-old chicks was also significantly impaired. This study confirms that a putative galactosyltransferase encoded bycj1136is involved in LOS biosynthesis and is important forC. jejunivirulence, as disruption of this gene and the resultant truncation of LOS affect both colonizationin vivoand invasivenessin vitro.


2000 ◽  
Vol 68 (9) ◽  
pp. 5167-5175 ◽  
Author(s):  
Ana María Cevallos ◽  
Najma Bhat ◽  
Renaud Verdon ◽  
Davidson H. Hamer ◽  
Barry Stein ◽  
...  

ABSTRACT The protozoan parasite Cryptosporidium parvum is a significant cause of diarrheal disease worldwide. Attachment to and invasion of host intestinal epithelial cells by C. parvumsporozoites are crucial steps in the pathogenesis of cryptosporidiosis. The molecular basis of these initial interactions is unknown. In order to identify putative C. parvum adhesion- and invasion-specific proteins, we raised monoclonal antibodies (MAbs) to sporozoites and evaluated them for inhibition of attachment and invasion in vitro. Using this approach, we identified two glycoproteins recognized by 4E9, a MAb which neutralized C. parvuminfection and inhibited sporozoite attachment to intestinal epithelial cells in vitro. 4E9 recognized a 40-kDa glycoprotein named gp40 and a second, >220-kDa protein which was identified as GP900, a previously described mucin-like glycoprotein. Glycoproteins recognized by 4E9 are localized to the surface and apical region of invasive stages and are shed in trails from the parasite during gliding motility. The epitope recognized by 4E9 contains α-N-acetylgalactosamine residues, which are present in a mucin-type O-glycosidic linkage. Lectins specific for these glycans bind to the surface and apical region of sporozoites and block attachment to host cells. The surface and apical localization of these glycoproteins and the neutralizing effect of the MAb and α-N-acetylgalactosamine-specific lectins strongly implicate these proteins and their glycotopes as playing a role in C. parvum-host cell interactions.


Nutrients ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 328 ◽  
Author(s):  
Claudio Salaris ◽  
Melania Scarpa ◽  
Marina Elli ◽  
Alice Bertolini ◽  
Simone Guglielmetti ◽  
...  

SARS-CoV-2 is a newly emerging virus that currently lacks curative treatments. Lactoferrin (LF) is a naturally occurring non-toxic glycoprotein with broad-spectrum antiviral, immunomodulatory and anti-inflammatory effects. In this study, we assessed the potential of LF in the prevention of SARS-CoV-2 infection in vitro. Antiviral immune response gene expression was analyzed by qRT-PCR in uninfected Caco-2 intestinal epithelial cells treated with LF. An infection assay for SARS-CoV-2 was performed in Caco-2 cells treated or not with LF. SARS-CoV-2 titer was determined by qRT-PCR, plaque assay and immunostaining. Inflammatory and anti-inflammatory cytokine production was determined by qRT-PCR. LF significantly induced the expression of IFNA1, IFNB1, TLR3, TLR7, IRF3, IRF7 and MAVS genes. Furthermore, LF partially inhibited SARS-CoV-2 infection and replication in Caco-2 intestinal epithelial cells. Our in vitro data support LF as an immune modulator of the antiviral immune response with moderate effects against SARS-CoV-2 infection.


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