Linear antigenic and immunogenic regions of human respiratory syncytial virus N protein

Leonov, Sergey; Waris, Matti; Norrby, Erling

doi:10.1099/0022-1317-76-2-357

Cited by 6 publications

(5 citation statements)

References 39 publications

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“…They are higher than those obtained for stable G protein genes, such as those of lyssaviruses (4), but lower than that of the hemagglutinin gene of influenza A virus, which is known to show rapid and temporal rather than geographical variations (19). In this respect, the molecular epidemiology of BRSV is intermediate between those of influenza B virus (6,78) HRSV N protein (positions 131 to 150) which was shown to be a linear antigenic domain (37). There is complete identity in this region between the two N proteins.…”

Section: Discussionmentioning

confidence: 82%

Evolution of Bovine Respiratory Syncytial Virus

Valarcher

Schelcher

Bourhy

2000

J Virol

164

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Until now, the analysis of the genetic diversity of bovine respiratory syncytial virus (BRSV) has been based on small numbers of field isolates. In this report, we determined the nucleotide and deduced amino acid sequences of regions of the nucleoprotein (N protein), fusion protein (F protein), and glycoprotein (G protein) of 54 European and North American isolates and compared them with the sequences of 33 isolates of BRSV obtained from the databases, together with those of 2 human respiratory syncytial viruses and 1 ovine respiratory syncytial virus. A clustering of BRSV sequences according to geographical origin was observed. We also set out to show that a continuous evolution of the sequences of the N, G, and F proteins of BRSV has been occurring in isolates since 1967 in countries where vaccination was widely used. The exertion of a strong positive selective pressure on the mucin-like region of the G protein and on particular sites of the N and F proteins is also demonstrated. Furthermore, mutations which are located in the conserved central hydrophobic part of the ectodomain of the G protein and which result in the loss of four Cys residues and in the suppression of two disulfide bridges and an ␣ helix critical to the three-dimensional structure of the G protein have been detected in some recent French BRSV isolates. This conserved central region, which is immunodominant in BRSV G protein, thus has been modified in recent isolates. This work demonstrates that the evolution of BRSV should be taken into account in the rational development of future vaccines. (38,39,40,49). These two related viruses share common epidemiological, clinical, and pathological characteristics. The respiratory syncytial viruses (RSV) are the most common and important cause of lower respiratory tract illness in cattle and young infants (71). More than 70% of calves exhibit a positive serological response against BRSV by the age of 12 months. Bovine respiratory syncytial virus (BRSV) and human respiratory syncytial virus (HRSV) are members of the genus Pneumovirus, subfamily Pneumovirinae, and family ParamyxoviridaeNeutralization tests (9) and reaction patterns with specific monoclonal antibodies (2, 48) have revealed that HRSV contains two major groups, A and B. The main differences between these two groups are located in the glycoprotein (G protein), while others are located in the fusion protein (F protein) and nucleoprotein (N protein) (48, 51). Subgroups within the G and F proteins of BRSV have been characterized more recently by serological analysis of a limited number of isolates and confirmed by phylogenetic analysis (20,54,60). Further studies of BRSV variability have focused on the G protein, which was shown to be the most variable protein and, with the F protein, one of the targets for neutralizing antibodies. A low percentage of sequence divergence between and within the G proteins of BRSV subgroups has been reported, suggesting that BRSV has the same extent of diversity as HRSV (15,21,36,44,66).The G protein is responsib...

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Section: Discussionmentioning

confidence: 82%

Evolution of Bovine Respiratory Syncytial Virus

Valarcher

Schelcher

Bourhy

2000

J Virol

164

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“…Use of overlapping synthetic peptides is useful to identify linear antigenic regions of viral proteins recognized by T and B lymphocytes [5,16,19,21,22]. EAV GL protein has been revealed as the major target of virus neutralization [3,9].…”

Section: Discussionmentioning

confidence: 99%

Identification of the Major Epitope in the GL Protein of Equine Arteritis Virus (EAV) Recognized by Antibody in EAV-infected Horses Using Synthetic Peptides.

Kondo¹,

Sugita

Fukunaga

et al. 1998

JES

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A panel of overlapping peptides covering the ectodomain of the GL protein of equine arteritis virus (EAV) was synthesized to identify the major epitope recognized by the EAV-seropositive horse sera by using enzyme-linked immunosorbent assay (ELISA). Three consecutive peptides, G15 (amino acid residues 75-90), G16 (79-94) and G17 (83-98), strongly reacted with 3 experimentally EAV-infected horse sera. G16 peptide was highly antigenic with all 8 EAVinfected horse sera tested. The ELISA absorbance values and the virus neutralization titers of antibodies in sera periodically collected from EAV-infected horses showed similar patterns. These results indicated that the major linear epitope of the EAV GL protein which was recognized with EAV-infected horse sera was mapped to residues from 83 to 90.

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“…However, close examination of the Western blot image presented in Fig. 2A of their manuscript shows a faint band of the expected size in lane 6, demonstrating possible reactivity between N protein [10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29] antisera and hRSV A2 lysate. We suspect that the use of hRSV recN protein in our assays increased sensitivity over whole-virus antigen and may account for this difference in results.…”

Section: Discussionmentioning

confidence: 99%

“…The hMPV rec⌬N protein was reciprocally recognized by both hMPV and hRSV antisera by Western blotting (data not shown), suggesting that a linear epitope(s) common to both viruses is present in this region. In fact, other studies have identified multiple linear epitopes within the carboxy domain of the hRSV N protein (21,26,27), and their potential common antigenicity with hMPV should be investigated. One possible explanation for the loss of immunoreactivity of the hMPV rec⌬N protein with antibody-positive human sera by EIA is that N protein antigenicity is conformation dependent, and the truncation of the amino-terminal portion of the protein changes its natural configuration, resulting in the loss of conformational epitopes or sequestering of linear epitopes.…”

Section: Discussionmentioning

confidence: 99%

Serologic Cross-Reactions between Nucleocapsid Proteins of Human Respiratory Syncytial Virus and Human Metapneumovirus

et al. 2015

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Human respiratory syncytial virus (hRSV) and human metapneumovirus (hMPV) share virologic and epidemiologic features and cause clinically similar respiratory illness predominantly in young children. In a previous study of acute febrile respiratory illness in Bangladesh, we tested paired serum specimens from 852 children presenting fever and cough for diagnostic increases in titers of antibody to hRSV and hMPV by enzyme immunoassay (EIA). Unexpectedly, of 93 serum pairs that showed a >4-fold increase in titers of antibody to hRSV, 24 (25.8%) showed a concurrent increase in titers of antibody to hMPV; of 91 pairs showing an increase to hMPV, 13 (14.3%) showed a concurrent increase to hRSV. We speculated that common antigens shared by these viruses explain this finding. Since the nucleocapsid (N) proteins of these viruses show the greatest sequence homology, we tested hyperimmune antisera prepared for each virus against baculovirus-expressed recombinant N (recN) proteins for potential cross-reactivity. The antisera were reciprocally reactive with both proteins. To localize common antigenic regions, we first expressed the carboxy domain of the hMPV N protein that was the most highly conserved region within the hRSV N protein. Although reciprocally reactive with antisera by Western blotting, this truncated protein did not react with hMPV IgG-positive human sera by EIA. Using 5 synthetic peptides that spanned the amino-terminal portion of the hMPV N protein, we identified a single peptide that was cross-reactive with human sera positive for either virus. Antiserum prepared for this peptide was reactive with recN proteins of both viruses, indicating that a common immunoreactive site exists in this region.H uman respiratory syncytial virus (hRSV) and human metapneumovirus (hMPV) are negative single-stranded, enveloped RNA viruses that are coclassified within the Pneumovirinae subfamily of the Paramyxoviridae. hRSV is the leading cause of severe lower respiratory tract infections in infants and young children and has been associated with community-acquired pneumonia in adults, with the highest mortality rates found among the hospitalized elderly and immunocompromised (1, 2, 3). hMPV was identified first in 2001 by van den Hoogen et al. (4) and subsequently has been shown to have clinical and epidemiological features similar to but distinct from those of hRSV (5, 6). Most hMPV infections occur within the first few years of life, usually later than those for hRSV, and cause 5 to 10% of respiratory infections in children requiring hospitalization, second only to hRSV (7). Both viruses are ubiquitous globally, and recent studies have documented a high prevalence of infection among children in less developed countries (8, 9). Clinical outcomes similar to those for hRSV have been described for hMPV infections in the frail elderly (10).The RNA genomes of hRSV and hMPV are complexed with nucleocapsid (N) protein that together serve as the templates for genome replication and transcription (11). The N protein is the most abundant...

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Linear antigenic and immunogenic regions of human respiratory syncytial virus N protein

Cited by 6 publications

References 39 publications

Evolution of Bovine Respiratory Syncytial Virus

Evolution of Bovine Respiratory Syncytial Virus

Identification of the Major Epitope in the GL Protein of Equine Arteritis Virus (EAV) Recognized by Antibody in EAV-infected Horses Using Synthetic Peptides.

Serologic Cross-Reactions between Nucleocapsid Proteins of Human Respiratory Syncytial Virus and Human Metapneumovirus

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