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Mumps virus
The mumps virus (MuV) is the virus that causes mumps. MuV contains a single-stranded, negative-sense genome made of ribonucleic acid (RNA). Its genome is about 15,000 nucleotides in length and contains seven genes that encode nine proteins. The genome is encased by a capsid that is in turn surrounded by a viral envelope. MuV particles, called virions, are pleomorphic in shape and vary in size from 100 to 600 nanometers in diameter. One serotype and twelve genotypes that vary in their geographic distribution are recognized. Humans are the only natural host of the mumps virus.
MuV replicates first by binding to the surface of cells, whereby its envelope merges with the host cell membrane to release the capsid inside of the cell. Once inside, the viral RNA-dependent RNA polymerase transcribes messenger RNA (mRNA) from the genome and later replicates the genome. After translation of viral proteins, virions are formed adjacent to the cell membrane, where they then leave the cell by budding from its surface, using the cell membrane as the envelope.
The mumps virus was first identified as the cause of mumps in 1934 and was first isolated in 1945. Within a few years after isolation, vaccines protecting against MuV infection had been developed. MuV was first recognized as a species in 1971, and it has been given the scientific name Orthorubulavirus parotitidis. It is assigned to the genus Orthorubulavirus in the subfamily Rubulavirinae, family Paramyxoviridae.
The mumps virus contains a nonsegmented, single-stranded, linear genome that is 15,384 nucleotides in length and made of ribonucleic acid (RNA). The genome has negative sense, so mRNA can be transcribed directly from the genome. Mumps virus encodes seven genes in the following order:
The SH protein is thought to be involved in blocking NF(α)-mediated apoptosis of the host cell, which is done as an antiviral response to suppress the spread of viruses, though SH is not necessary for replication since MuVs engineered without SH are still able to replicate. The V protein is also involved in evading host antiviral responses by means of inhibiting production and signalling of interferons. Unlike the other proteins, the I protein's function is unknown.
The genome of the mumps virus is encased by N proteins to form a flexible, loosely coiled helical ribonucleoprotein (RNP) complex consisting of the genome surrounded by a nucleocapsid that RdRp is bound to. RNPs are surrounded by an envelope, a lipid membrane, which contains two types of spikes on its surface that correspond to the HN and F glycoproteins. M proteins are found on the inner side of the envelope, connecting the envelope to the RNP. Virions vary in size from 100 to 600 nanometers (nm) in diameter and are pleomorphic in shape.
MuV first interacts with a host cell by binding to its surface via the HN protein's receptor, sialic acid, which binds to sialic acid receptors on the surface of host cells. Following attachment, the F protein is triggered and begins fusing the viral envelope with the host cell's membrane. The F protein does so by changing from a metastable state to refolding to a more stable hairpin structure, which allows the contents of the virion, including the RNP, to be released into the host cell's cytoplasm.
Upon entering the host cell, the RdRp begins transcribing mRNA from the genome inside the RNP. Transcription starts at or near the 3'-end (usually pronounced "three prime end") at a promoter region and moves sequentially toward the 5'-end. One mRNA strand is transcribed for each gene, and it is necessary for all genes sequentially before a gene to be transcribed for that gene to be transcribed. Genes closer to the 3'-end are transcribed at the highest frequency, decreasing in frequency as RdRp approaches the 5'-end. RdRp synthesizes a cap on the 5'-end of the mRNA and a polyadenylated tail on the 3'-end consisting of hundreds of consecutive adenines. Once a gene has been transcribed, RdRp releases it into the cytoplasm for subsequent translation of viral proteins by host ribosomes. The V and P proteins are encoded by the same gene, so while transcribing mRNA, RdRp edits the mRNA by inserting two non-templated guanines into the mRNA to transcribes mRNA for the P protein.
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Mumps virus
The mumps virus (MuV) is the virus that causes mumps. MuV contains a single-stranded, negative-sense genome made of ribonucleic acid (RNA). Its genome is about 15,000 nucleotides in length and contains seven genes that encode nine proteins. The genome is encased by a capsid that is in turn surrounded by a viral envelope. MuV particles, called virions, are pleomorphic in shape and vary in size from 100 to 600 nanometers in diameter. One serotype and twelve genotypes that vary in their geographic distribution are recognized. Humans are the only natural host of the mumps virus.
MuV replicates first by binding to the surface of cells, whereby its envelope merges with the host cell membrane to release the capsid inside of the cell. Once inside, the viral RNA-dependent RNA polymerase transcribes messenger RNA (mRNA) from the genome and later replicates the genome. After translation of viral proteins, virions are formed adjacent to the cell membrane, where they then leave the cell by budding from its surface, using the cell membrane as the envelope.
The mumps virus was first identified as the cause of mumps in 1934 and was first isolated in 1945. Within a few years after isolation, vaccines protecting against MuV infection had been developed. MuV was first recognized as a species in 1971, and it has been given the scientific name Orthorubulavirus parotitidis. It is assigned to the genus Orthorubulavirus in the subfamily Rubulavirinae, family Paramyxoviridae.
The mumps virus contains a nonsegmented, single-stranded, linear genome that is 15,384 nucleotides in length and made of ribonucleic acid (RNA). The genome has negative sense, so mRNA can be transcribed directly from the genome. Mumps virus encodes seven genes in the following order:
The SH protein is thought to be involved in blocking NF(α)-mediated apoptosis of the host cell, which is done as an antiviral response to suppress the spread of viruses, though SH is not necessary for replication since MuVs engineered without SH are still able to replicate. The V protein is also involved in evading host antiviral responses by means of inhibiting production and signalling of interferons. Unlike the other proteins, the I protein's function is unknown.
The genome of the mumps virus is encased by N proteins to form a flexible, loosely coiled helical ribonucleoprotein (RNP) complex consisting of the genome surrounded by a nucleocapsid that RdRp is bound to. RNPs are surrounded by an envelope, a lipid membrane, which contains two types of spikes on its surface that correspond to the HN and F glycoproteins. M proteins are found on the inner side of the envelope, connecting the envelope to the RNP. Virions vary in size from 100 to 600 nanometers (nm) in diameter and are pleomorphic in shape.
MuV first interacts with a host cell by binding to its surface via the HN protein's receptor, sialic acid, which binds to sialic acid receptors on the surface of host cells. Following attachment, the F protein is triggered and begins fusing the viral envelope with the host cell's membrane. The F protein does so by changing from a metastable state to refolding to a more stable hairpin structure, which allows the contents of the virion, including the RNP, to be released into the host cell's cytoplasm.
Upon entering the host cell, the RdRp begins transcribing mRNA from the genome inside the RNP. Transcription starts at or near the 3'-end (usually pronounced "three prime end") at a promoter region and moves sequentially toward the 5'-end. One mRNA strand is transcribed for each gene, and it is necessary for all genes sequentially before a gene to be transcribed for that gene to be transcribed. Genes closer to the 3'-end are transcribed at the highest frequency, decreasing in frequency as RdRp approaches the 5'-end. RdRp synthesizes a cap on the 5'-end of the mRNA and a polyadenylated tail on the 3'-end consisting of hundreds of consecutive adenines. Once a gene has been transcribed, RdRp releases it into the cytoplasm for subsequent translation of viral proteins by host ribosomes. The V and P proteins are encoded by the same gene, so while transcribing mRNA, RdRp edits the mRNA by inserting two non-templated guanines into the mRNA to transcribes mRNA for the P protein.