Exploring the Pathogenic Potential of Vibrio vulnificus Isolated from Seafood Harvested along the Mangaluru Coast, India

It has been observed that not all strains of Vibrio vulnificus are virulent. Determining the virulence of strains that are frequently present in seafood is of significance for ensuring seafood safety. This study is an attempt to predict the virulence of seafood-borne V. vulnificus isolated along the Mangaluru Coast, India. The isolates tested possessed a vcgC gene sequence with high similarity to that in the clinical strain. Transcriptional analysis of core virulence genes in seafood isolate E4010 showed the phenomenon of contact-mediated expression of rtxA1 which correlated well with the actin disintegration and cytotoxicity. These results suggest that the seafood isolates tested in this study possess a functional RtxA1 which could help in initiating the infection. However, other putative virulence genes such as vvpE encoding an extracellular protease, vvhA encoding hemolysin, flp encoding tad pilin and ompU encoding fibronectin-binding protein were also constitutively expressed. Virulence-associated attributes such as cytotoxicity and adherence matched the response of the clinical strain (p > 0.05). On the other hand, the environmental strains showed higher serum sensitivity compared with the clinical strain. These findings show that the part of virulence attributes required for the disease process might be intact in these isolates.

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Isolation of an amino-terminal fibronectin-binding protein on human U937 cells and rat peritoneal macrophages.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)50620-2 ◽

1992 ◽

Vol 267 (6) ◽

pp. 3968-3975

Author(s):

S.D. Blystone ◽

J.E. Kaplan

Keyword(s):

Binding Protein ◽

Peritoneal Macrophages ◽

U937 Cells ◽

Amino Terminal ◽

Fibronectin Binding Protein ◽

Fibronectin Binding

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Association between Resistance to Erythromycin and the Presence of the Fibronectin Binding Protein F1 Gene, prtF1, in Streptococcus pyogenes Isolates from German Pediatric Patients

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.49.7.2990-2993.2005 ◽

2005 ◽

Vol 49 (7) ◽

pp. 2990-2993 ◽

Cited By ~ 4

Author(s):

Maria Haller ◽

Kirsten Fluegge ◽

Sandra Jasminder Arri ◽

Brit Adams ◽

Reinhard Berner

Keyword(s):

Streptococcus Pyogenes ◽

Pediatric Patients ◽

Group A Streptococcus ◽

Binding Protein ◽

Macrolide Resistance ◽

Group A ◽

Fibronectin Binding Protein ◽

Fibronectin Binding ◽

Cell Invasiveness

ABSTRACT A total of 301 German pediatric group A streptococcus isolates were screened for the presence of macrolide resistance and the fibronectin binding protein F1 gene (prtF1) encoding an adhesin and cell invasiveness protein. The prtF1 gene was present significantly more often among macrolide-resistant isolates. The majority of these were not clonally related.

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Protective Immunity againstStreptococcus pyogenesChallenge in Mice after Immunization with Fibronectin‐Binding Protein

The Journal of Infectious Diseases ◽

10.1086/498162 ◽

2005 ◽

Vol 192 (12) ◽

pp. 2081-2091 ◽

Cited By ~ 35

Author(s):

Yutaka Terao ◽

Shigefumi Okamoto ◽

Kosuke Kataoka ◽

Shigeyuki Hamada ◽

Shigetada Kawabata

Keyword(s):

Protective Immunity ◽

Binding Protein ◽

Fibronectin Binding Protein ◽

Fibronectin Binding

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Borrelia burgdorferi Lacking BBK32, a Fibronectin-Binding Protein, Retains Full Pathogenicity

Infection and Immunity ◽

10.1128/iai.02035-05 ◽

2006 ◽

Vol 74 (6) ◽

pp. 3305-3313 ◽

Cited By ~ 68

Author(s):

Xin Li ◽

Xianzhong Liu ◽

Deborah S. Beck ◽

Fred S. Kantor ◽

Erol Fikrig

Keyword(s):

Life Cycle ◽

Borrelia Burgdorferi ◽

Deletion Mutant ◽

Binding Protein ◽

Kanamycin Resistance ◽

Binding Activity ◽

Mammalian Host ◽

Wild Type ◽

Fibronectin Binding Protein ◽

Fibronectin Binding

ABSTRACT BBK32, a fibronectin-binding protein of Borrelia burgdorferi, is one of many surface lipoproteins that are differentially expressed by the Lyme disease spirochete at various stages of its life cycle. The level of BBK32 expression in B. burgdorferi is highest during infection of the mammalian host and lowest in flat ticks. This temporal expression profile, along with its fibronectin-binding activity, strongly suggests that BBK32 may play an important role in Lyme pathogenesis in the host. To test this hypothesis, we constructed an isogenic BBK32 deletion mutant from wild-type B. burgdorferi B31 by replacing the BBK32 gene with a kanamycin resistance cassette through homologous recombination. We examined both the wild-type strain and the BBK32 deletion mutant extensively in the experimental mouse-tick model of the Borrelia life cycle. Our data indicated that B. burgdorferi lacking BBK32 retained full pathogenicity in mice, regardless of whether mice were infected artificially by syringe inoculation or naturally by tick bite. The loss of BBK32 expression in the mutant had no adverse effect on spirochete acquisition (mouse-to-tick) and transmission (tick-to-mouse) processes. These results suggest that additional B. burgdorferi proteins can complement the function of BBK32, fibronectin binding or otherwise, during the natural spirochete life cycle.

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Contribution of fibronectin-binding protein to pathogenesis ofStreptococcus equissp. zooepidemicus

Pathogens and Disease ◽

10.1111/2049-632x.12029 ◽

2013 ◽

Vol 67 (3) ◽

pp. 174-183 ◽

Cited By ~ 10

Author(s):

Li Yi ◽

Yang Wang ◽

Zhe Ma ◽

Hui Zhang ◽

Yue Li ◽

...

Keyword(s):

Binding Protein ◽

Fibronectin Binding Protein ◽

Fibronectin Binding

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Complete Genome Sequence of Bacteriophage EFC1 Infecting Enterococcus Faecalis From Chicken

10.21203/rs.3.rs-1118970/v1 ◽

2021 ◽

Author(s):

Qi Wang ◽

Na Liu

Keyword(s):

Enterococcus Faecalis ◽

Virulence Genes ◽

Large Subunit ◽

Antibiotic Resistance Genes ◽

Lytic Phage ◽

High Similarity ◽

Protein Coding ◽

Circular Dna ◽

Intron Structure ◽

Comparative Phylogenetic Analysis

Abstract In response to Enterococcus faecalis infection of chicken origin, a multi host lytic phage, EFC1 was isolated and characterized the double-stranded circular DNA genome with size of 56099 bp, containing 89 predicted protein coding genes as well as 2 tRNAs involved in intron, structure, transcription, packaging, DNA replication, modification, lysis. Observation of the structure by electron microscopy and comparative phylogenetic analysis of terminase large subunit showed that the phage EFC1 belongs to a new member of Siphoviridae, which is relatively distantly related to its high similarity phages. The phage EFC1 has no relevant virulence genes and antibiotic resistance genes.

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Evidence for Association of Vibrio Echinoideorum with Tissue Necrosis on Body Shell of the Green Sea Urchin Strongylocentrotus Droebachiensis

10.21203/rs.3.rs-1085079/v1 ◽

2021 ◽

Author(s):

Jonathan Hira ◽

Klara Stensvåg

Keyword(s):

Sea Urchin ◽

Virulence Genes ◽

Vibrio Vulnificus ◽

Sea Urchins ◽

Opportunistic Pathogen ◽

Significant Degree ◽

Strongylocentrotus Droebachiensis ◽

Host Immune System ◽

Progressive Development ◽

Green Sea Urchin

Abstract “Sea urchin lesion syndrome” is known as sea urchins disease with the progressive development of necrotic epidermal tissue and loss of external organs, including appendages on the outer body surface. Recently, a novel strain, Vibrio echinoideorum has been isolated from the lesions of green sea urchin (Strongylocentrotus droebachiensis), an economically important mariculture species in Norway. V. echinoideorum has not been reported elsewhere in association of with green sea urchin lesion syndrome. Therefore, in this study, an immersion based bacterial challenge experiment was performed to expose sea urchins (wounded and non-wounded) to V. echinoideorum, thereby mimicking a nearly natural host-pathogen interaction under controlled conditions. This infection experiment demonstrated that only the injured sea urchins developed the lesion to a significant degree when exposed to V. echinoideorum. Pure cultures of the employed bacterial strain was recovered from the infected animals and its identity was confirmed by the MALDI-TOF MS spectra profiling. Additionally, the hemolytic phenotype of V. echinoideorum substantiated its virulence potential towards the host, and this was also supported by the cytolytic effect on red spherule cells of sea urchins. Furthermore, the genome sequence of V. echinoideorum was assumed to encode potential virulence genes and were subjected for in silico comparison with the established virulence factors of Vibrio vulnificus and Vibrio tasmaniensis. This comparative virulence profile provided novel insights about virulence genes and their putative functions related to chemotaxis, adherence, invasion, evasion of the host immune system, and damage of host tissue and cells. Thus, it supports the pathogenicity of V. echinoideorum. In conclusion, the interaction of V. echinoideorum with injured sea urchins appears to be essential for the development of lesion syndrome and therefore, revealing its potentiality as an opportunistic pathogen.

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