Prediction and Identification of Potential Immunodominant Epitopes in Glycoproteins B, C, E, G, and I of Herpes Simplex Virus Type 2

Abstract

<jats:p>Twenty B candidate epitopes of glycoproteins B (gB2), C (gC2), E (gE2), G (gG2), and I (gI2) of herpes simplex virus type 2 (HSV-2) were predicted using DNAstar, Biosun, and Antheprot methods combined with the polynomial method. Subsequently, the biological functions of the peptides were tested via experiments<jats:italic>in vitro</jats:italic>. Among the 20 epitope peptides, 17 could react with the antisera to the corresponding parent proteins in the EIA tests. In particular, five peptides, namely, gB2<jats:sub>466–473</jats:sub>(EQDRKPRN), gC2<jats:sub>216–223</jats:sub>(GRTDRPSA), gE2<jats:sub>483–491</jats:sub>(DPPERPDSP), gG2<jats:sub>572–579</jats:sub>(EPPDDDDS), and gI2<jats:sub>286-295</jats:sub>(CRRRYRRPRG) had strong reaction with the antisera. All conjugates of the five peptides with the carrier protein BSA could stimulate mice into producing antibodies. The antisera to these peptides reacted strongly with the corresponding parent glycoproteins during the Western Blot tests, and the peptides reacted strongly with the antibodies against the parent glycoproteins during the EIA tests. The antisera against the five peptides could neutralize HSV-2 infection<jats:italic>in vitro</jats:italic>, which has not been reported until now. These results suggest that the immunodominant epitopes screened using software algorithms may be used for virus diagnosis and vaccine design against HSV-2.</jats:p>

Linear Multiepitope (Glyco)peptides for Type-Specific Serology of Herpes Simplex Virus (HSV) Infections

“…This is the first time that these epitopes have been identified by serology with clinical samples and thus represent novel candidates for further selection (see below). However, parts of the last sequence gE2 451–545 have been previously predicted to show antigenicity . In the case of gG the glycoproteins gG1 and gG2 differ significantly in terms of size and sequence, but scattered reactivity to both gG1 and gG2 was found on sequences with homology (Figure i,j).…”

“…For comparison, data in Figure d from gG2 were extracted from Clo et al No significant serum reactivity was found on gH peptides (Figure k,l). Surprisingly, a large difference was found between gI1 and gI2 (Figure m,n) with intense serum responses on gI2 peptides, despite a significant sequence homology.…”

Identification and immunogenic potential of B cell epitopes of outer membrane protein OmpF of Aeromonas hydrophila in translational fusion with a carrier protein

“…Epitope-based vaccines have for long stood out as promising vaccine candidates against diverse pathogens (Christy et al 2012;Hurtgen et al 2012;Pan et al 2012;Kunthalert et al 2013;Rojas-Caraballo et al 2014) and have forayed their way in human clinical trials as well (Iinuma et al 2014). Other than helping to focus on and thereby narrowing down the specificity of immune response, they also leave room for chimera generation including multiple epitopes from same as well as different and slightly more immunogenic antigens.…”

InSilico Identification and Conservation Analysis of B-cell and T-Cell Epitopes of Hepatitis C Virus 3a Genotype Enveloped Glycoprotein 2From Pakistan: A Step Towards Heterologous Vaccine Design

“…Many neutralizing antibodies against HCV gpE2 gene are reported; however these antibodies differ in their mechanism of neutralization and are mostly homologus in action ( 17 ). Recent studies have proved that predicted epitopes by different online tools shows immunogenicity when experimentally checked in herpes simplex virus, influenza A virus , and Vibriomimicus ( 30 , 31 ). The human antibodies raised against HCV gpE2 epitopes do not offer protection against multiple viral infections; the preseason may be related to either genetic variations among viral strains particularly within the hyper variable region-1 (HVR-1), low titers of anti-gpE2 antibodies, or interference of non-neutralizing antibodies with the function of neutralizing antibodies ( 32 ).…”