Alphavirus Pathogenesis and Immunity

Griffin, Diane E.

doi:10.1007/978-1-4757-0785-4_8

Cited by 59 publications

(42 citation statements)

References 214 publications

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“…The most intensively studied alphaviruses, including Venezuelan and eastern equine encephalitis viruses and SIN, develop a biphasic disease in infected amplification hosts that is characterized by high-titer viremia before the appearance of virus in the brain and encephalitis development (13,16,17). Viremia is also a prerequisite of a natural transmission cycle of alphaviruses that is required for infection of mosquito vectors.…”

Section: Discussionmentioning

confidence: 99%

“…In mosquitoes, alphaviruses cause a persistent, life-long infection that has little effect on the viability of their vectors (47). Infected vertebrates, in contrast, develop an acute disease, often characterized by high-titer viremia before either virus clearance by the immune system or host death (17,19). Accordingly, alphaviruses usually establish a persistent or chronic infection in cultured mosquito cells and exhibit a highly cytopathic phenotype in cell cultures of mammalian and avian origin (49).…”

mentioning

confidence: 99%

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Inhibition of Transcription and Translation in Sindbis Virus-Infected Cells

Gorchakov

Frolova

Frolov

2005

J Virol

128

211

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Inhibition of Transcription and Translation in Sindbis Virus-Infected Cells

Gorchakov

Frolova

Frolov

2005

J Virol

128

211

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“…In mosquitoes, they cause persistent, lifelong infection and do not cause noticeable effects on the biological functions of the vector. In vertebrates, alphavirus infection is characterized by high-titer viremia, which is required for virus transmission to mosquitoes during the next blood meal (4,5). Many alphaviruses also enter the brain, where they replicate to very high titers and cause severe meningoencephalitis with frequent lethality or neurological sequelae (6).…”

mentioning

confidence: 99%

The Amino-Terminal Domain of Alphavirus Capsid Protein Is Dispensable for Viral Particle Assembly but Regulates RNA Encapsidation through Cooperative Functions of Its Subdomains

Lulla

Kim

Frolova

et al. 2013

J Virol

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Venezuelan equine encephalitis virus (VEEV) is a pathogenic alphavirus, which circulates in the Central, South, and North Americas, including the United States, and represents a significant public health threat. In recent years, strong progress has been made in understanding the structure of VEEV virions, but the mechanism of their formation has yet to be investigated. In this study, we analyzed the functions of different capsid-specific domains and its amino-terminal subdomains in viral particle formation. Our data demonstrate that VEEV particles can be efficiently formed directly at the plasma membrane without cytoplasmic nucleocapsid preassembly. The entire amino-terminal domain of VEEV capsid protein was found to be dispensable for particle formation. VEEV variants encoding only the capsid's protease domain efficiently produce genome-free VEEV virus-like particles (VLPs), which are very similar in structure to the wild-type virions. The amino-terminal domain of the VEEV capsid protein contains at least four structurally and functionally distinct subdomains, which mediate RNA packaging and the specificity of packaging in particular. The most positively charged subdomain is a negative regulator of the nucleocapsid assembly. The three other subdomains are not required for genome-free VLP formation but are important regulators of RNA packaging. Our data suggest that the positively charged surface of the VEEV capsid-specific protease domain and the very amino-terminal subdomain are also involved in interaction with viral RNA and play important roles in RNA encapsidation. Finally, we show that VEEV variants with mutated capsid acquire compensatory mutations in either capsid or nsP2 genes.

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“…The E1 protein has traditionally been associated with haemagglutination of erythrocytes (Dalrymple et al, 1976), is relatively conserved, and probably associated with cross-protection among alphaviruses that are not cross-neutralizing (Griffin, 1986). Identification of epitopes on the E1 glycoproteins of VEEV , SFV (Boere et al, 1984) and Western equine encephalitis virus (Hunt & Roehrig, 1985) have demonstrated five or six epitopes with a mixture of neutralizing and haemagglutinationinhibiting MAb activities.…”

Section: Discussionmentioning

confidence: 99%

“…Recovery from experimental alphavirus infections correlates best with the development of antiviral antibody, rather than virus-specific cellular immunity (Griffin, 1986). The availability of monoclonal antibodies (MAbs) to a number of alphaviruses has made possible a more detailed analysis of the specificities, biological activities and efficiencies of protective antibodies.…”

Section: Introductionmentioning

confidence: 99%

Monoclonal Antibodies to the E1 and E2 Glycoproteins of Sindbis Virus: Definition of Epitopes and Efficiency of Protection from Fatal Encephalitis

Mendoza

Stanley

Griffin

1988

Journal of General Virology

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SUMMARYProtection of mice from fatal neuroadapted Sindbis virus encephalitis can be accomplished by passive transfer of monoclonal antibodies (MAbs) to either the E1 or E2 glycoprotein of Sindbis virus. Both neutralizing and non-neutralizing MAbs can be protective. To define further the characteristics of MAbs that provide protection from fatal disease, antigenic epitopes on the E1 and E2 glycoproteins were identified using a competitive binding enzyme immunoassay. Four distinct epitopes on E1 and three on E2 were defined. MAbs to all E1 epitopes, both neutralizing (three) and nonneutralizing (one) protected mice from fatal encephalitis. MAbs to the E2 neutralizing epitopes (two) protected mice from fatal encephalitis while those to the nonneutralizing epitope did not. The efficiency of protection from fatal Sindbis virus encephalitis of four neutralizing and non-neutralizing protective anti-E1 and anti-E2 MAbs representing different epitopes was compared. The neutralizing MAbs (against epitopes E2-ab, E2-c and El-c) gave 50% protection at lower doses (2 to 20 gg) than the non-neutralizing MAb representing epitope El-e (150 gg) when given before virus challenge. When given after virus challenge, MAbs to E2-ab and E2-c protected at lower doses (0,03 to 0.3 Ixg) than did either MAbs to El-c (> 100 gg) or El-e (10 p~g). The MAbs to El-e, E2-ab and E2-c were required in larger amounts to afford protection before than after challenge, while the opposite was true for MAb to E 1-c.

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Alphavirus Pathogenesis and Immunity

Cited by 59 publications

References 214 publications

Inhibition of Transcription and Translation in Sindbis Virus-Infected Cells

Inhibition of Transcription and Translation in Sindbis Virus-Infected Cells

The Amino-Terminal Domain of Alphavirus Capsid Protein Is Dispensable for Viral Particle Assembly but Regulates RNA Encapsidation through Cooperative Functions of Its Subdomains

Monoclonal Antibodies to the E1 and E2 Glycoproteins of Sindbis Virus: Definition of Epitopes and Efficiency of Protection from Fatal Encephalitis

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