Priming and induction of anti-rotavirus antibody response by synthetic peptides derived from VP7 and VP4

Ijaz, M. Khalid; Alkarmi, T.; El-Mekki, A.W.; Galadari, Sehamuddin; Dar, F.K.; Babiuk, Lorne A.

doi:10.1016/0264-410x(95)98252-6

Cited by 10 publications

(5 citation statements)

References 47 publications

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“…To overcome these limitations, foreign epitopes have been grafted onto VLPs by chemical linkage and especially by genetic engineering. 5,6 A critical disadvantage of chimeric VLPs is the limited size of the epitopes that can be recombinantly inserted. The inserted peptide should disturb neither the three-dimensional folding nor the quaternary arrangement of the protein particle.…”

Section: Introductionmentioning

confidence: 99%

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Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

et al. 2004

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Protein assemblies with a high degree of repetitiveness and organization are known to induce strong immune responses. For that reason they have been postulated for the design of subunit vaccines by means of protein engineering. The enzyme lumazine synthase from Brucella spp. (BLS) is highly immunogenic, presumably owing to its homodecameric arrangement and remarkable thermodynamic stability. Structural analysis has shown that it is possible to insert foreign peptides at the ten amino terminus of BLS without disrupting its general folding. These peptides would be displayed to the immune system in a highly symmetric three-dimensional array. In the present work, BLS has been used as a protein carrier of foreign peptides. We have established a modular system to produce chimeric proteins decorated with ten copies of a desired peptide as long as 27 residues and have shown that their folding and stability is similar to that of the wild-type protein. The knowledge about the mechanisms of dissociation and unfolding of BLS allowed the engineering of polyvalent chimeras displaying different predefined peptides on the same molecular scaffold. Moreover, the reassembly of mixtures of chimeras at different steps of the unfolding process was used to control the stoichiometry and spatial arrangement for the simultaneous display of different peptides on BLS. This strategy would be useful for vaccine development and other biomedical applications.

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Section: Introductionmentioning

confidence: 99%

“…To overcome these limitations, foreign epitopes have been grafted onto VLPs by chemical linkage and especially by genetic engineering 5, 6. A critical disadvantage of chimeric VLPs is the limited size of the epitopes that can be recombinantly inserted.…”

Section: Introductionmentioning

confidence: 99%

Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

et al. 2004

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“…Synthetic peptides are also useful to develop efficient SARS therapeutic drugs. For example, peptide immunization can generate specific Abs [16–18]. If a peptide containing a neutralizing epitope, which can inhibit the interaction between virus spike protein and its ACE2 receptor.…”

Section: Discussionmentioning

confidence: 99%

Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential

Shi

et al. 2005

FEBS Letters

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The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) is an important viral structural protein. Based on bioinformatics analysis, 10 antigenic peptides derived from the S protein sequence were selected and synthesized. The antigenicity and immunoreactivity of all the peptides were tested in vivo and in vitro. Four peptides (P6, P8, P9 and P10) which contain B cell epitopes of the S protein were identified, and P8 peptide was confirmed in vivo to have a potential in serological diagnosis. By using a syncytia formation model, we tested the neutralization ability of all 10 peptides and their corresponding antibodies. It is interesting to find that P8 and P9 peptides inhibited syncytia formation, suggesting that the P8 and P9 spanning regions may provide a good target for anti-SARS-CoV drug design. Our data suggest that we have identified peptides derived from the S protein of SARS-CoV, which are useful for SARS treatment and diagnosis.

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“…This is the first report of MAbs produced against VP7 of Nebraska calf diarrhea strain BRV by using purified viral particles as immunogen. MAbs produced by using synthetic peptide from VP7 as the immunogen for MAb production were unable to detect antirotavirus antibodies as tested by ELISA (12). In another study that used a VP7 peptide-VP6 conjugate as the immunogen, the MAbs produced provided less protection than those obtained by using BRV as the immunogen (13).…”

Section: Discussionmentioning

confidence: 99%

Development, Characterization, and Diagnostic Applications of Monoclonal Antibodies against Bovine Rotavirus

Al-Yousif

Al-Majhdi

Chard-Bergstrom

et al. 2000

Clin Diagn Lab Immunol

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Hybridomas secreting monoclonal antibodies (MAbs) against the Nebraska calf diarrhea strain of bovine rotavirus (BRV) were characterized. Indirect fluorescent-antibody assay, immunodot assay, and immunoprecipitation were used to select hybridomas that produced anti-BRV MAbs. Seven of the MAbs were shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot assay to be reactive with the BRV outer capsid protein, VP7, which has a molecular mass of 37.5 kDa. None of the seven MAbs were reactive with canine rotavirus, bovine coronavirus, or uninfected Madin-Darby bovine kidney cells. Two clones, 8B4 (immunoglobulin G2a [IgG2a]) and 2B11 (IgG1), were found suitable for use in an antigen capture enzyme-linked immunosorbent assay for detecting BRV in bovine fecal samples. Both were subtype A specific (G6 subtype) but did not react with all isolates of BRV group A.Rotavirus, a member of the Reoviridae family, is an important cause of gastroenteritis in young children, calves, monkeys, chickens, pigs, sheep, and horses (1,14). It is nonenveloped and has double-shelled capsids surrounding a genome of 11 double-stranded RNA segments. Seven serological groups of rotavirus, A to G, have been identified, but only groups A, B, C, D, and G have been characterized well (15). Each group can be differentiated by polyacrylamide gel electrophoretic mobilities (2, 23).Among the seven serogroups, group A rotavirus has been studied in greatest detail, and it is the serogroup most commonly found in cattle worldwide. The virus is composed of a core surrounded by VP6, the major inner capsid protein. The outer capsid layers of infectious bovine rotavirus (BRV) particles contain two proteins, VP4 and VP7. The VP4 (P) types are spike protein encoded by RNA segment 4 (19, 21). They constitute important outer capsid proteins with various functions such as hemagglutinating activity (22) and neutralization activity (10,25,37), and when cleaved by trypsin into VP5 and VP8, they enhance the infectivity of the virus. There is evidence that rotavirus VP4 sequences are diverse (32). Using monoclonal antibodies (MAbs) against VP4, diversity has been shown in the amino acid sequences of epitopes that are critical for cross-reaction and neutralization of rotaviruses (18,19,22,33). Both VP4 and VP7 are associated with stimulation of serotype-specific antibodies and in vivo protection. Serotypes 1 to 4 of VP7 are glycosylated (6). Proteins other than VP4 and VP7, such as VP6, associated with stimulation of serotypespecific antibodies, may participate in protection against BRV infection; however, neutralizing antibodies in vitro have been shown to be specific against VP4 and VP7. Protection against rotavirus infection appears to rely mainly on stimulation of neutralizing antibodies against the outer capsid proteins, VP4 and VP7 (27).Many established protocols and commercial kits are available to detect rotavirus infection for human diagnostic medical applications including electron microscopy and enzyme-linked immunosorbent assay (E...

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Priming and induction of anti-rotavirus antibody response by synthetic peptides derived from VP7 and VP4

Cited by 10 publications

References 47 publications

Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

Synthetic peptides derived from SARS coronavirus S protein with diagnostic and therapeutic potential

Development, Characterization, and Diagnostic Applications of Monoclonal Antibodies against Bovine Rotavirus

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