Nonstructural Protein 2 (NS2) of Respiratory Syncytial Virus (RSV) Detected by an Antipeptide Serum

Weber, Elke; Humbert, B; Streckert, H. J.; Werchau, H

doi:10.1159/000196385

Cited by 24 publications

(16 citation statements)

References 16 publications

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“…The NS2 protein also appears to be a transcriptional inhibitor but at a lower level than the NS1 protein [7]. The NS2 protein colocalizes with the P and N proteins in infected cells [164] but does not coprecipitate with any viral protein [42]. These proteins are not essential for virus replication in vitro, although the growth of recombinant HRSV and BRSV lacking one or other of these proteins is attenuated in cell culture [20,115,137].…”

Section: Non-structural Proteins Ns1 and Ns2mentioning

confidence: 99%

Bovine respiratory syncytial virus infection

Valarcher¹,

2007

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-Bovine respiratory syncytial virus (BRSV) belongs to the pneumovirus genus within the family Paramyxoviridae and is a major cause of respiratory disease in young calves. BRSV is enveloped and contains a negative sense, single-stranded RNA genome encoding 11 proteins. The virus replicates predominantly in ciliated respiratory epithelial cells but also in type II pneumocytes. It appears to cause little or no cytopathology in ciliated epithelial cell cultures in vitro, suggesting that much of the pathology is due to the host's response to virus infection. RSV infection induces an array of pro-inflammatory chemokines and cytokines that recruit neutrophils, macrophages and lymphocytes to the respiratory tract resulting in respiratory disease. Although the mechanisms responsible for induction of these chemokines and cytokines are unclear, studies on the closely related human (H)RSV suggest that activation of NF-κB via TLR4 and TLR3 signalling pathways is involved. An understanding of the mechanisms by which BRSV is able to establish infection and induce an inflammatory response has been facilitated by advances in reverse genetics, which have enabled manipulation of the virus genome. These studies have demonstrated an important role for the non-structural proteins in anti-interferon activity, a role for a virokinin, released during proteolytic cleavage of the fusion protein, in the inflammatory response and a role for the SH and the secreted form of the G protein in establishing pulmonary infection. Knowledge gained from these studies has also provided the opportunity to develop safe, stable, live attenuated virus vaccine candidates.

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Section: Non-structural Proteins Ns1 and Ns2mentioning

confidence: 99%

Bovine respiratory syncytial virus infection

Valarcher¹,

2007

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“…The NS2 protein also appears to be a transcriptional inhibitor but at a lower level than is the NS1 protein (1). The NS2 protein colocalizes with the P and N proteins in infected cells (60) but does not coprecipitate with any viral protein (19). In addition, the NS1 and NS2 proteins of BRSV and HRSV mediate resistance to the antiviral action of alpha/beta inferferons (IFN-␣/␤) (3,42).…”

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confidence: 99%

Role of Alpha/Beta Interferons in the Attenuation and Immunogenicity of Recombinant Bovine Respiratory Syncytial Viruses Lacking NS Proteins

Valarcher

Furze

Wyld

et al. 2003

J Virol

139

133

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Bovine respiratory syncytial virus (BRSV) is an enveloped, nonsegmented, negative-stranded RNA virus and is a major cause of respiratory disease in young calves (44). BRSV is closely related to human RSV (HRSV), which is a major cause of respiratory disease in young children (10), and the epidemiology and pathogenesis of infection with these viruses are similar (44). These features make BRSV infection in calves a good model for the study of HRSV. HRSV and BRSV belong to the Pneumovirus genus within the Paramyxoviridae family. One of the major differences between this genus and all the other Paramyxoviridae is the presence of two nonstructural (NS) genes called NS1 and NS2. These genes code for two proteins, which are abundantly transcribed in virus-infected cells. Comparison of the sequence of the NS proteins of BRSV with that of HRSV subgroup A and B reveals amino acid identities of 69 and 68% for the NS1 protein and 84 and 83% for the NS2 protein, respectively (8, 39).The role(s) of the NS proteins is not fully defined. They are not essential for virus replication in vitro, although the growth of recombinant HRSV and BRSV lacking these proteins is attenuated in cell culture (8,25,42,51). There is evidence that the HRSV NS1 protein coprecipitates with the M protein (19), and in experiments using HRSV minigenomes, the NS1 protein appears to be a strong inhibitor of viral RNA transcription and replication (1). The NS2 protein also appears to be a transcriptional inhibitor but at a lower level than is the NS1 protein (1). The NS2 protein colocalizes with the P and N proteins in infected cells (60) but does not coprecipitate with any viral protein (19). In addition, the NS1 and NS2 proteins of BRSV and HRSV mediate resistance to the antiviral action of alpha/beta inferferons (IFN-␣/␤) (3, 42).Anti-IFN activity has been described for accessory proteins for a number of other negative-stranded RNA viruses. Of those characterized to date, some block the IFN response by hindering the late-stage activation of antiviral genes. For example, the C protein of Sendai virus inhibits STAT1 activation by hampering phosphorylation and by increasing instability (21, 64) and the V protein of simian virus 5 inhibits the activation of IFN-responsive genes by targeting STAT1 for proteasome-mediated degradation (13). Other viral accessory proteins, such as influenza A virus NS1 protein and Bunyamwera virus NSs protein, inhibit the production of IFN-␣/␤ (58, 61).

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“…The deduced sequences, however, did not provide obvious clues to the function of NS proteins in the virus life cycle. The HRSV NS1 protein was reported to be associated with the M protein, while the NS2 protein did not show any detectable association with RSV structural proteins, indicating distinct functions of NS1 and NS2 (16,47). An inhibitory function of NS1 in virus RNA transcription and RNP replication was recently suggested by experiments in which artificial HRSV minigenomes were grown in the absence or presence of NS1.…”

mentioning

confidence: 99%

Bovine Respiratory Syncytial Virus Nonstructural Proteins NS1 and NS2 Cooperatively Antagonize Alpha/Beta Interferon-Induced Antiviral Response

Schlender¹,

Bossert²,

Buchholz

et al. 2000

J Virol

217

194

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Bovine respiratory syncytial virus (BRSV) is a major etiological agent of respiratory tract disease in calves and results in substantial economic loss (40,45). The immune response and pathology in calves mimic symptoms caused by human respiratory syncytial virus (HRSV), which remains the leading cause of serious bronchiolitis and pneumonia in infants and young children throughout the world (9). Molecular cloning has confirmed a very close relationship between BRSV and HRSV and has revealed substantial differences from other members of the Paramyxoviridae family, leading to the establishment of the Pneumovirus genus within the Paramyxoviridae family (36, 37).As with all members of the order Mononegavirales, the 15-kb genomic RNA of RSV is contained in a ribonucleoprotein (RNP) complex which serves as a template for sequential transcription of genes (25, 49). Eleven proteins are expressed from 10 transcription units, which are arranged in the order 3Ј-NS1-NS2-N-P-M-SH-G-F-M2-L-5Ј (5, 9, 30, 31). The proteins encoded include five RNP-associated proteins, namely, the nucleoprotein N, the phosphoprotein P, the large catalytic subunit L of the RNA polymerase, and a transcription elongation factor (M2-1) encoded by the first of two overlapping open reading frames of the M2 gene (8,17,27,38). The second open reading frame of the M2 transcription unit (M2-2) was reported to encode a nonessential protein (1) which is probably involved in the regulation of RNA synthesis (4, 28). Three viral proteins are associated with the viral envelope, namely, the fusion protein F, the putative attachment protein G, and a small hydrophobic protein SH.The presence of two nonstructural protein genes, NS1 and NS2, at the 3Ј-terminal position of the genome distinguishes pneumoviruses from all other members of the Mononegavirales. Due to the 3Ј-proximal location, the NS genes are abundantly transcribed. The encoded proteins have been demonstrated in infected cells (10,16). The BRSV NS1 and NS2 genes encode polypeptides of 136 and 124 amino acids, respectively. Comparison with NS proteins of HRSV subgroup A and B proteins revealed amino acid identities of 69 and 68% for NS1 proteins and 84 and 83%, for NS2 proteins, respectively (5, 34). The deduced sequences, however, did not provide obvious clues to the function of NS proteins in the virus life cycle. The HRSV NS1 protein was reported to be associated with the M protein, while the NS2 protein did not show any detectable association with RSV structural proteins, indicating distinct functions of NS1 and NS2 (16,47). An inhibitory function of NS1 in virus RNA transcription and RNP replication was recently suggested by experiments in which artificial HRSV minigenomes were grown in the absence or presence of NS1. In the same study, an inhibitory but far less pronounced effect was also observed for NS2 (3).Recently established protocols for recovery of infectious minus-strand RNA viruses from cDNA (11) have allowed the generation of recombinant HRSV (8, 29) and BRSV (5) and allowed researchers to...

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Nonstructural Protein 2 (NS2) of Respiratory Syncytial Virus (RSV) Detected by an Antipeptide Serum

Cited by 24 publications

References 16 publications

Bovine respiratory syncytial virus infection

Bovine respiratory syncytial virus infection

Role of Alpha/Beta Interferons in the Attenuation and Immunogenicity of Recombinant Bovine Respiratory Syncytial Viruses Lacking NS Proteins

Bovine Respiratory Syncytial Virus Nonstructural Proteins NS1 and NS2 Cooperatively Antagonize Alpha/Beta Interferon-Induced Antiviral Response

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