Comparative nucleotide and deduced amino acid sequence analyses of the RNA and proteins of several fixed rabies virus strains have allowed detailed characterization of structural-functional relations of individual virus components. Several unique features of rabies viruses have been deduced from the complete nucleotide sequences of four of the five genes and the four intergenic regions of the genome. The most extensively analyzed rabies virus gene has been that of the surface glycoprotein. Direct comparisons between the deduced amino acid sequences of glycoprotein variants have led to the location of specific sites on the glycoprotein that bind virus-neutralizing antibodies and to the identification of an epitope correlating with viral pathogenicity. Structural requirements for immunogenic activity within the glycoprotein have also been investigated. This article presents an overview of the molecular biology of rabies viruses and describes the current state of knowledge of immunobiologic characteristics of different rabies virus components.

Amino Acid Sequence↗

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Antigenic diversity of the glycoprotein and nucleocapsid proteins of rabies and rabies-related viruses: implications for epidemiology and control of rabies.

Rabies virus-specific monoclonal antibodies (MAbs) have served to describe operationally the topography of the antigenic structure of the glycoprotein and nucleocapsid proteins of rabies virus. With the use of nucleocapsid protein-specific MAbs and cleavage fragments of the nucleoprotein and phosphoprotein, it has been possible to identify the chemical structure of two antigenic sites of the nucleoprotein and one antigenic site of the phosphoprotein. Antisera produced to synthetic peptides that make up the structure of these antigenic sites exhibited reactivities similar to those of MAbs. Analysis of a large number of isolates of rabies virus from different animal species and from different geographic locations revealed that rabies viruses differ considerably in their antigenic structure and can be identified according to their characteristic reactivity patterns with MAbs. Analysis of field virus isolates has also revealed that strains of rabies virus generally are associated with only one or a few major mammalian hosts within any given geographic area. Protection experiments in mice have not demonstrated correlations between protective activity and degree of antigenic difference between the vaccine strain and the challenge virus. Therefore, changes in antigenic structure, as determined by analysis with rabies virus-specific MAbs, cannot predict whether a given rabies vaccine will protect against a particular field virus.

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Suggestive evidence for an oncorna-virus-specific DNA polymerase from C-type particles of bovine leukosis.

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Genotypic and phenotypic diversity of rabies virus variants involved in human rabies: implications for postexposure prophylaxis.

OBJECTIVES: Rabies virus variants associated with silver-haired bats (SHBRV) are responsible for most recent human rabies cases in the United States, which are not associated with a history of exposure. We compared their genotype and phenotype with those of dog rabies virus (DRV) variants, the classic cause of rabies in humans, to determine whether differences in these strains might have ramifications for therapeutic intervention, particularly vaccination. METHODS: Eleven silver-haired bat and 8 dog rabies virus isolates were characterized by sequencing the glycoprotein gene, by assessing their ability to replicate in neuronal versus nonneuronal cultures at optimal and suboptimal temperatures, by assessing their pathogenicity in mice, and by determining the resistance of these viruses to therapeutic immunization with commercial vaccines. RESULTS: SHBRV isolates were less genetically diverse, less neuronal cell specific, more temperature sensitive, but as pathogenic, on average, as DRV isolates. Immune protection was equivalent for SHBRV and DRV strains of similar pathogenicity. CONCLUSIONS: SHBRV strains have unique characteristics that may explain their exceptional association with human rabies but have little bearing on their lethality in mice. The pathogenicity of a particular virus, rather than its antigenic makeup, determines the outcome of immunization.

Amino Acid Sequence↗

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Breakage in alpha-helix: a recognition site for anti-rabies virus ribonucleoprotein antibody.

Peptides composed of variants of a B-cell epitope followed by a T-cell determinant of rabies virus ribonucleoprotein (RNP) have been synthesized to elicit antibody production in mice. Conformation of the peptides was characterized by secondary structural prediction and circular dichroism measurements. It was found that only synthetic peptides with disrupted helical structure in the antigenic region were active on immunoblot assay, performed against a natural anti-protein monoclonal antibody (MAb) and provoked virus-neutralizing antibody production.

Amino Acid Sequence↗