Conformational epitope mapping of OmpC, a major cell surface antigen from Salmonella typhi

Arockiasamy, A.; Murthy, G. S.; Rukmini, M. R.; Baalaji, N. Sundara; Katpally, Umesh; Krishnaswamy, S.

doi:10.1016/j.jsb.2004.03.011

Cited by 19 publications

(13 citation statements)

References 17 publications

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“…Omp C of Salmonella has been purified using salt extraction procedures [19], and its epitopes have been mapped [20]. It is found to be a trimer made of 16 stranded β -barrel monomers and is a major cell surface antigen from the human pathogen Salmonella typhi .…”

Section: Resultsmentioning

confidence: 99%

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Cloning, Sequencing andIn SilicoAnalysis of Omp C ofSalmonellaTyphimurium

Jha

Kumar

Saxena

et al. 2012

ISRN Veterinary Science

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SalmonellaTyphimurium is an important pathogen having a broad host range. In human population it causes mostly gastroenteritis but there are reports in which it was found to be responsible to cause several lethal diseases like endocarditis and meningitis. Poultry products are the major sources of this organism in India as these are consumed at various stages of cooking. The available vaccines have their own limitations such as short-term immunity. Outer membrane proteins have shown some promising potential, so in the present study Omp C ofSalmonellaTyphimurium was cloned and sequenced to explore the possibility of development of r-DNA vaccine againstSalmonellaTyphimurium for poultry. The sequence of Omp C was studied for antigenic indexing, epitope mapping, and MHC mapping using various bioinformatic tools. The ORF analysis revealed a complete coding region of approximately 1000 bp. Five major and 13 minor B-cell epitopes were identified having an antigenic index of 1.7. The sequences also showed major histocompatibility complex (MHC) class I and class II binding region indicating a potential of eliciting cell-mediated immune response. The findings indicate that Omp C may be proven as promising candidate for development of r-DNA vaccine againstSalmonellaTyphimurium.

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Section: Resultsmentioning

confidence: 99%

“…The assembly of trimer and the stability of the β -barrel have been found to be important for epitope presentation. The Salmonella -specific conformational epitope was found to be more stable than in case of Enterobacteria [20]. …”

Section: Resultsmentioning

confidence: 99%

Cloning, Sequencing andIn SilicoAnalysis of Omp C ofSalmonellaTyphimurium

Jha

Kumar

Saxena

et al. 2012

ISRN Veterinary Science

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“…It is found to be a trimer made of 16 stranded β-barrel monomers and is a major cell surface antigen from the human pathogen Salmonella typhi. [3132] Sequencing revealed that the C-terminus of Omp 28 has typical characteristic of Omps. The last residue at the C-terminus, phenylalanine has been reported to be highly conserved among outer membrane proteins and is essential for stability and correct assembly of protein into the outer membrane.…”

Section: Resultsmentioning

confidence: 99%

Cloning, sequencing, and in silico characterization of Omp 28 of Salmonella Typhi (strain MTCC 733) to develop r-DNA vaccine for typhoid fever

Saxena¹,

Tamuly²,

Saxena³

2012

J Nat Sc Biol Med

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Background:Typhoid is one of the most important diseases of human beings caused by Salmonella Typhi. There are many vaccine reported against Salmonella Typhi, but search for new candidate vaccine antigens is still going on because presently available vaccines have several limitations such as short-term immunity, high cost, and allergic reaction. Several approaches such as subunit vaccines, Vi polysaccharide, mutant vaccines, and r-DNA vaccines have been tested. r- DNA vaccines have shown some promising potential (targeted Omp). Omp 28 had shown very promising results and suggests that it should be used in further studies of animal protection against the disease.Objective:Cloning, Sequencing and In silico analysis of Omp 28 gene to develop r-DNA vaccine of S. Typhi.Materials and Methods:Omp 28 is made up of three identical subunits of 9.6 kDa showing PCR amplicon of 330 bp which has been cloned in the pJET vector. Recombinant clones has been sequenced, and data submitted to NCBI. Secondary structure was deduced by the Chou Fasman and Garnier method. The sequence of Omp 28 was studied for antigenic indexing, epitope mapping, and MHC mapping using various bioinformatics tool.Results and Conclusion:The sequence of Omp 28 has been assigned accession no GQ 907044.1 by NCBI. Secondary structure has shown it has more alpha region. Hydrophobic plot and surface probability plot shows most amino acids are surface exposed which is a requirement to develop a r-DNA vaccine. Antigenic sites are located within surface exposed regions and eight antigenic determinants are present in Omp 28. On Prosite analysis of Protein shown two motifs i.e. anaphylatoxin domain signature motif at position 219-252 and other one was iron sulphur binding region signature motif at position 36-44. On epitope analysis total six major B cell epitopes were observed which can provoke humoral immunity. On T cell epitope mapping several major epitopes has been found in case of MHC class I and MHC class II. It indicates that Omp 28 can provoke cell mediated as well as humoral immunity and can be proven a promising candidates of Salmonella Typhi.

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“…Compared to E coli, Salmonella specific conformational epitope is more stable in nature (Arockiasamy et al, 2004). The results from in silico analysis indicate that OmpF is having better properties on comparison with OmpC protein, with high immunogenic potential.…”

Section: T-cell Epitope Predictionmentioning

confidence: 97%