scholarly journals Complete Genome Sequences of Campylobacter jejuni Strains OD267 and WP2202 Isolated from Retail Chicken Livers and Gizzards Reveal the Presence of Novel 116-Kilobase and 119-Kilobase Megaplasmids with Type VI Secretion Systems

2016 ◽  
Vol 4 (5) ◽  
Author(s):  
Daya Marasini ◽  
Mohamed K. Fakhr

Genome sequences of Campylobacter jejuni strains OD267 and WP2202, isolated from chicken livers and gizzards, showed the presence of novel 116-kb and 119-kb megaplasmids, respectively. The two megaplasmids carry a type VI secretion system and tetracycline resistance genes. These are the largest sequenced Campylobacter plasmids to date.

2017 ◽  
Vol 5 (47) ◽  
Author(s):  
Daya Marasini ◽  
Mohamed K. Fakhr

ABSTRACT We report the complete genome sequences of multidrug-resistant Campylobacter jejuni and Campylobacter coli isolated from retail turkey and pork, respectively. The chromosomes of these two isolates contained type VI secretion system genes. The two isolates also harbored large plasmids with antimicrobial resistance genes possibly contributing to their multidrug resistance.


2017 ◽  
Vol 5 (47) ◽  
Author(s):  
Daya Marasini ◽  
Mohamed K. Fakhr

ABSTRACT Genome sequences of Campylobacter jejuni FJ3124 and ZP3204 isolated from retail chicken gizzards and Campylobacter jejuni TS1218 isolated from retail chicken showed the presence of 1,694,324-, 1,763,161-, and 1,762,596-bp circular chromosomes, respectively. Campylobacter jejuni ZP3204 and TS1218 harbored large tetracycline resistance plasmids with type IV secretion systems.


2021 ◽  
Vol 12 ◽  
Author(s):  
Luca Robinson ◽  
Janie Liaw ◽  
Zahra Omole ◽  
Dong Xia ◽  
Arnoud H. M. van Vliet ◽  
...  

The Type VI Secretion System (T6SS) has important roles relating to bacterial antagonism, subversion of host cells, and niche colonisation. Campylobacter jejuni is one of the leading bacterial causes of human gastroenteritis worldwide and is a commensal coloniser of birds. Although recently discovered, the T6SS biological functions and identities of its effectors are still poorly defined in C. jejuni. Here, we perform a comprehensive bioinformatic analysis of the C. jejuni T6SS by investigating the prevalence and genetic architecture of the T6SS in 513 publicly available genomes using C. jejuni 488 strain as reference. A unique and conserved T6SS cluster associated with the Campylobacter jejuni Integrated Element 3 (CJIE3) was identified in the genomes of 117 strains. Analyses of the T6SS-positive 488 strain against the T6SS-negative C. jejuni RM1221 strain and the T6SS-positive plasmid pCJDM202 carried by C. jejuni WP2-202 strain defined the “T6SS-containing CJIE3” as a pathogenicity island, thus renamed as Campylobacter jejuni Pathogenicity Island-1 (CJPI-1). Analysis of CJPI-1 revealed two canonical VgrG homologues, CJ488_0978 and CJ488_0998, harbouring distinct C-termini in a genetically variable region downstream of the T6SS operon. CJPI-1 was also found to carry a putative DinJ-YafQ Type II toxin-antitoxin (TA) module, conserved across pCJDM202 and the genomic island CJIE3, as well as several open reading frames functionally predicted to encode for nucleases, lipases, and peptidoglycan hydrolases. This comprehensive in silico study provides a framework for experimental characterisation of T6SS-related effectors and TA modules in C. jejuni.


2014 ◽  
Vol 7 (8) ◽  
Author(s):  
Bahman Abdi Hachesoo ◽  
Rahem Khoshbakht ◽  
Hassan Sharifi Yazdi ◽  
Mohammad Tabatabaei ◽  
Saeid Hosseinzadeh ◽  
...  

2021 ◽  
Vol 12 ◽  
Author(s):  
Luca Robinson ◽  
Janie Liaw ◽  
Zahra Omole ◽  
Dong Xia ◽  
Arnoud H. M. van Vliet ◽  
...  

2017 ◽  
Author(s):  
Maximilian Brackmann ◽  
Jing Wang ◽  
Marek Basler

AbstractSecretion systems are essential for bacteria to survive and manipulate their environment. The bacterial Type VI Secretion System (T6SS) generates the force needed for protein translocation by the contraction of a long polymer called sheath, which is composed of interconnected VipA/VipB subunits forming a six-start helix. The mechanism of T6SS sheath contraction and the structure of its extended state are unknown. Here we show that elongating the N-terminal VipA linker or eliminating charge of a specific VipB residue abolished sheath contraction and delivery of effectors into target cells. The assembly of the non-contractile sheaths was dependent on the baseplate component TssE and mass-spectrometry analysis identified Hcp, VgrG and other components of the T6SS baseplate specifically associated with stable non-contractile sheaths. The ability to lock T6SS in the pre-firing state opens new possibilities for understanding its mode of action.


2017 ◽  
Vol 83 (13) ◽  
Author(s):  
Peng Li ◽  
Lisa N. Kinch ◽  
Ann Ray ◽  
Ankur B. Dalia ◽  
Qian Cong ◽  
...  

ABSTRACT Acute hepatopancreatic necrosis disease (AHPND) is a newly emerging shrimp disease that has severely damaged the global shrimp industry. AHPND is caused by toxic strains of Vibrio parahaemolyticus that have acquired a “selfish plasmid” encoding the deadly binary toxins PirAvp/PirBvp. To better understand the repertoire of virulence factors in AHPND-causing V. parahaemolyticus, we conducted a comparative analysis using the genome sequences of the clinical strain RIMD2210633 and of environmental non-AHPND and toxic AHPND isolates of V. parahaemolyticus. Interestingly, we found that all of the AHPND strains, but none of the non-AHPND strains, harbor the antibacterial type VI secretion system 1 (T6SS1), which we previously identified and characterized in the clinical isolate RIMD2210633. This finding suggests that the acquisition of this T6SS might confer to AHPND-causing V. parahaemolyticus a fitness advantage over competing bacteria and facilitate shrimp infection. Additionally, we found highly dynamic effector loci in the T6SS1 of AHPND-causing strains, leading to diverse effector repertoires. Our discovery provides novel insights into AHPND-causing pathogens and reveals a potential target for disease control. IMPORTANCE Acute hepatopancreatic necrosis disease (AHPND) is a serious disease that has caused severe damage and significant financial losses to the global shrimp industry. To better understand and prevent this shrimp disease, it is essential to thoroughly characterize its causative agent, Vibrio parahaemolyticus. Although the plasmid-encoded binary toxins PirAvp/PirBvp have been shown to be the primary cause of AHPND, it remains unknown whether other virulent factors are commonly present in V. parahaemolyticus and might play important roles during shrimp infection. Here, we analyzed the genome sequences of clinical, non-AHPND, and AHPND strains to characterize their repertoires of key virulence determinants. Our studies reveal that an antibacterial type VI secretion system is associated with the AHPND strains and differentiates them from non-AHPND strains, similar to what was seen with the PirA/PirB toxins. We propose that T6SS1 provides a selective advantage during shrimp infections.


2008 ◽  
Vol 190 (13) ◽  
pp. 4584-4595 ◽  
Author(s):  
Jagjit S. Ludu ◽  
Olle M. de Bruin ◽  
Barry N. Duplantis ◽  
Crystal L. Schmerk ◽  
Alicia Y. Chou ◽  
...  

ABSTRACT Francisella tularensis is a highly infectious, facultative intracellular bacterial pathogen that is the causative agent of tularemia. Nearly a century ago, researchers observed that tularemia was often fatal in North America but almost never fatal in Europe and Asia. The chromosomes of F. tularensis strains carry two identical copies of the Francisella pathogenicity island (FPI), and the FPIs of North America-specific biotypes contain two genes, anmK and pdpD, that are not found in biotypes that are distributed over the entire Northern Hemisphere. In this work, we studied the contribution of anmK and pdpD to virulence by using F. novicida, which is very closely related to F. tularensis but which carries only one copy of the FPI. We showed that anmK and pdpD are necessary for full virulence but not for intracellular growth. This is in sharp contrast to most other FPI genes that have been studied to date, which are required for intracellular growth. We also showed that PdpD is localized to the outer membrane. Further, overexpression of PdpD affects the cellular distribution of FPI-encoded proteins IglA, IglB, and IglC. Finally, deletions of FPI genes encoding proteins that are homologues of known components of type VI secretion systems abolished the altered distribution of IglC and the outer membrane localization of PdpD.


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