Protective immunization against Epstein-Barr virus-induced disease in cottontop tamarins using the virus envelope glycoprotein gp340 produced from a bovine papillomavirus expression vector

Finerty, S.; Tarlton, John F; Mackett, Mike; Conway, Margaret J; Arrand, John R.; Watkins, P. E.; Morgan, Andrew

doi:10.1099/0022-1317-73-2-449

Cited by 50 publications

(24 citation statements)

References 21 publications

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“…EBV gp350 protects cottontop marmosets from B cell lymphomas when challenged with high titers of EBV [2]. Numerous studies have shown that gp350 purified from cells [3], [4], expressed as a recombinant protein [5], [6], or expressed from an adenovirus [7] or vaccinia vector [8] can protect marmosets from EBV lymphomas. Vaccinia virus expressing gp350 induced EBV neutralizing antibody in seronegative children and a showed a trend toward protection from EBV infection [9].…”

Section: Introductionmentioning

confidence: 99%

Soluble Rhesus Lymphocryptovirus gp350 Protects against Infection and Reduces Viral Loads in Animals that Become Infected with Virus after Challenge

et al. 2011

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Epstein-Barr virus (EBV) is a human lymphocryptovirus that is associated with several malignancies. Elevated EBV DNA in the blood is observed in transplant recipients prior to, and at the time of post-transplant lymphoproliferative disease; thus, a vaccine that either prevents EBV infection or lowers the viral load might reduce certain EBV malignancies. Two major approaches have been suggested for an EBV vaccine- immunization with either EBV glycoprotein 350 (gp350) or EBV latency proteins (e.g. EBV nuclear antigens [EBNAs]). No comparative trials, however, have been performed. Rhesus lymphocryptovirus (LCV) encodes a homolog for each gene in EBV and infection of monkeys reproduces the clinical, immunologic, and virologic features of both acute and latent EBV infection. We vaccinated rhesus monkeys at 0, 4 and 12 weeks with (a) soluble rhesus LCV gp350, (b) virus-like replicon particles (VRPs) expressing rhesus LCV gp350, (c) VRPs expressing rhesus LCV gp350, EBNA-3A, and EBNA-3B, or (d) PBS. Animals vaccinated with soluble gp350 produced higher levels of antibody to the glycoprotein than those vaccinated with VRPs expressing gp350. Animals vaccinated with VRPs expressing EBNA-3A and EBNA-3B developed LCV-specific CD4 and CD8 T cell immunity to these proteins, while VRPs expressing gp350 did not induce detectable T cell immunity to gp350. After challenge with rhesus LCV, animals vaccinated with soluble rhesus LCV gp350 had the best level of protection against infection based on seroconversion, viral DNA, and viral RNA in the blood after challenge. Surprisingly, animals vaccinated with gp350 that became infected had the lowest LCV DNA loads in the blood at 23 months after challenge. These studies indicate that gp350 is critical for both protection against infection with rhesus LCV and for reducing the viral load in animals that become infected after challenge. Our results suggest that additional trials with soluble EBV gp350 alone, or in combination with other EBV proteins, should be considered to reduce EBV infection or virus-associated malignancies in humans.

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Section: Introductionmentioning

confidence: 99%

Soluble Rhesus Lymphocryptovirus gp350 Protects against Infection and Reduces Viral Loads in Animals that Become Infected with Virus after Challenge

et al. 2011

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“…The efficacy of potential vaccines has been widely tested in the cotton-top tamarin, Saguinus oedipus. Preparations of EBV membrane glycoproteins gp340 and 220, together with various adjuvants, have proved successful in preventing strain B95-8-induced disease in this species Morgan et al, 1989;Finerty et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Persistent Epstein--Barr virus infection in the common marmoset (Callithrix jacchus)

Cox

Chang

Karran

et al. 1996

Journal of General Virology

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Epstein-Barr virus (EBV) infection of the common marmoset causes long-term infection, with production of antibodies to virus-induced antigens, without clinical illness. Attempts to show the presence of EBV DNA in saliva of infected animals by PCR were initially unsuccessful, although slot-blot hybridization analysis demonstrated that viral DNA was present. Further investigations showed that most samples ofpilocarpineinduced saliva, and 33 % of the samples of whole mouth fluids (WMF) tested, were inhibitory to PCR. Similar results were found using human WMF. A method of assessing samples of marmoset WMF for the presence of EBV, by PCR using an EBV BamHI W probe, and removing inhibition with Chelex 100, is described. A total of 202 samples from 21 EBV infected, and seven non-infected animals was tested. Five seropositive animals shed virus on every occasion, and 15 intermittently. Two marmosets, infected as neonates, showed progressively increasing humoral responses to viral antigens, and shed virus on every occasion tested over 3 years. When mated with uninfected animals, the latter seroconverted 4 and 6 weeks later, respectively, and later shed virus into their WMF. The naturally infected animals were paired with naive marmosets, and were able to pass on infection. These results establish that long-term, permissive EBV infection occurs in the common marmoset, and demonstrate again the similarities in the response to EBV between marmoset and man.

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“…Increasing numbers of observations indicated that immunization with gp350 could provide Electronic supplementary material The online version of this article (doi:10.1007/s00253-015-7027-x) contains supplementary material, which is available to authorized users. protection from EBV-induced lymphomas in animal models (Finerty et al 1992(Finerty et al , 1994Sashihara et al 2011). Results from the first clinical trial showed that gp350-based vaccination elicited neutralizing antibodies and protected the subjects from EBV infection (Gu et al 1995).…”

Section: Introductionmentioning

confidence: 99%

Expression and immunogenic characterization of recombinant gp350 for developing a subunit vaccine against Epstein-Barr virus

Wang

Jiang

Han

et al. 2015

Appl Microbiol Biotechnol

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Epstein-Barr virus (EBV) is a ubiquitous human herpesvirus that is linked to the development of various malignancies. There is an urgent need for effective vaccines against EBV. EBV envelope glycoprotein gp350 is an attractive candidate for a prophylactic vaccine. This study was undertaken to produce the truncated (codons 1-443) gp350 protein (gp350(1-443)) in Pichia pastoris and evaluate its immunogenicity. The gp350(1-443) protein was expressed as a secretory protein with an N-terminal His-tag in P. pastoris and purified through Ni-NTA chromatography. Immunization with the recombinant gp350(1-443) could elicit high levels of gp350(1-443)-specific antibodies in mice. Moreover, gp350(1-443)-immunized mice developed strong lymphoproliferative and Th1/Th2 cytokine responses. Furthermore, the recombinant gp350(1-443) could stimulate CD4(+) and CD8(+) T cell responses in vaccinated mice. Collectively, these findings demonstrated that the yeast-expressed gp350(1-443) retained strong immunogenicity. This study will provide a useful source for developing EBV subunit vaccine candidates.

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Protective immunization against Epstein-Barr virus-induced disease in cottontop tamarins using the virus envelope glycoprotein gp340 produced from a bovine papillomavirus expression vector

Cited by 50 publications

References 21 publications

Soluble Rhesus Lymphocryptovirus gp350 Protects against Infection and Reduces Viral Loads in Animals that Become Infected with Virus after Challenge

Soluble Rhesus Lymphocryptovirus gp350 Protects against Infection and Reduces Viral Loads in Animals that Become Infected with Virus after Challenge

Persistent Epstein--Barr virus infection in the common marmoset (Callithrix jacchus)

Expression and immunogenic characterization of recombinant gp350 for developing a subunit vaccine against Epstein-Barr virus

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