Protection from mouse hepatitis virus type 3-induced acute disease by an anti-nucleoprotein monoclonal antibody

Lecomte, Jacqueline; Cainelli-Gebara, V. C. B.; Mercier, Ginette; Mansour, Suzanne L.; Talbot, Pierre J.; Lussier, G; Oth, D.

doi:10.1007/bf01310740

Cited by 63 publications

(62 citation statements)

References 17 publications

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“…In an MHV experimental system, the monoclonal antibodies raised against the M protein were able to neutralize infectivity in vitro, thus protecting the host mice against lethal challenge 3., 11.. Two antigenic sites have been detected in the exterior region and could be potentially involved in virus-host interaction supported by our experimental data.…”

Section: Discussionsupporting

confidence: 73%

“…The M protein might be related to the viral infectivity through binding to the viral S protein, and then subsequently binding to the host cellular receptor(s) and helping with the membrane fusion 1., 3., 11.. The N-terminal exterior region of the M protein is postulated to be responsible for its important roles in the pathogen-host interaction and membrane fusion with the host cell.…”

Section: Discussionmentioning

confidence: 99%

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The M Protein of SARS-CoV: Basic Structural and Immunological Properties

Wen

Tang

et al. 2003

Genomics, Proteomics &Amp; Bioinformatics

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We studied structural and immunological properties of the SARS-CoV M (membrane) protein, based on comparative analyses of sequence features, phylogenetic investigation, and experimental results. The M protein is predicted to contain a triple-spanning transmembrane (TM) region, a single N-glycosylation site near its N-terminus that is in the exterior of the virion, and a long C-terminal region in the interior. The M protein harbors a higher substitution rate (0.6% correlated to its size) among viral open reading frames (ORFs) from published data. The four substitutions detected in the M protein, which cause non-synonymous changes, can be classified into three types. One of them results in changes of pI (isoelectric point) and charge, affecting antigenicity. The second changes hydrophobicity of the TM region, and the third one relates to hydrophilicity of the interior structure. Phylogenetic tree building based on the variations of the M protein appears to support the non-human origin of SARS-CoV. To investigate its immunogenicity, we synthesized eight oligopeptides covering 69.2% of the entire ORF and screened them by using ELISA (enzyme-linked immunosorbent assay) with sera from SARS patients. The results confirmed our predictions on antigenic sites.

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Section: Discussionsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 99%

The M Protein of SARS-CoV: Basic Structural and Immunological Properties

Wen

Tang

et al. 2003

Genomics, Proteomics &Amp; Bioinformatics

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“…Data on the role of this protein in immunity against MHV are somewhat confusing. Whereas antibodies to N reportedly have no neutralizing activity in vitro Talbot et al, 1984;Nakanaga et al, 1986;Gilmore et al, 1987) a MAb to the protein prevented the c.p.e, of MHV in L cells (Lecomte et al, 1987). This antibody as well as another, non-neutralizing MAb (Nakanaga et al, 1986) protected mice from acute disease, in contrast to the lack of passive in vivo protection reported with several other anti-N antibodies (Hasony & MacNaughton, 1981 ;Buchmeier et al, 1984;Talbot et al, 1984).…”

Section: Discussioncontrasting

confidence: 46%

“…Antibodies directed against the N protein do not neutralize virus in vitro but in some cases passive transfer of monoclonal antibodies (MAbs) specific to the N protein of MHV-2 (Nakanaga et al, 1986) and MHV-3 (Lecomte et al, 1987) protects mice from a lethal MHV infection. Furthermore, some MAbs directed against the M protein, in one case with virus-neutralizing activity in vitro, were shown to protect mice against a lethal MHV-4-induced hepatitis (Fleming et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vectors protect mice against a lethal infection

Wesseling

Godeke

Schijns

et al. 1993

Journal of General Virology

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Infection with the mouse hepatitis coronavirus (MHV) provides an excellent model for the study of viral diseases of the central nervous system and the gastrointestinal tract. With the ultimate aim of studying mucosal immunity to MHV we have cloned the genes encoding the structural proteins of MHV strain A59 (MHV-A59) into the E3 region of a human adenovirus type 5 vector. Infection of HeLa cells with the resulting recombinant adenoviruses AdMHVS, AdMHVN and AdMHVM revealed the correct expression of the spike (S), nucleocapsid (N) and membrane (M) proteins, respectively. Intraperitoneal inoculation of BALB/c mice with the recombinant viruses elicited serum antibodies which specifically recognized the respective MHV proteins in an immunoprecipitation assay. Only antibodies to the S protein neutralized MHV-A59 in vitro but titres were low. When analysed by ELISA or by immunofluorescence only the antibody response to the N protein was significant; weak responses or no detectable response at all were found for S and M, respectively. Upon intracerebral challenge with a lethal dose of MHV-A59 we found that a significant fraction of animals vaccinated with adenovirus vectors expressing either the S protein or N protein were protected. This protective effect was significantly stronger when the animals were given a booster immunization with the same vector prior to challenge. No protection was induced by AdMHVM. Interestingly, enhanced protection resulted when AdMHVS and AdMHVN were applied in combination as compared to survival after single immunizations. The results indicate that both the N and S proteins generate a protective immune response and suggest that this response is enhanced by combined expression of the two proteins.

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“…However, the relative contributions of each effector mechanism are not clear. For example, passive transfer of both neutralizing monoclonal antibodies (MAb) specific for the S protein (Buchmeier et al, 1984) and non-neutralizing MAb specific for the matrix (M), nucleocapsid (N) and haemagglutinin--esterase (HE) proteins provides protection from acute disease (Fleming et al, 1988 ;Lecomte et al, 1987;Nakanaga et al, 1986;Yokomori et al, 1992). Whereas neutralizing antibodies appear to protect via a direct reduction in virus replication, protection by non-neutralizing MAb is not associated with a dramatic decrease in virus replication.…”

Section: Introductionmentioning

confidence: 99%

The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response

Bergmann¹,

Qin²,

Lin

et al. 1996

Journal of General Virology

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Cytotoxic T lymphocyte (CTL) activity specific for mouse hepatitis virus (MHV) JHM strain (JHMV or MHV-4) was examined using in vitro stimulated spleen cells derived from immunized C57BL/6 (H-2 b) mice. Target cells infected with JHMV were specifically recognized; however, analysis of target cells expressing the virus structural proteins via recombinant vaccinia viruses showed no recognition of the viral nucleocapsid (N), membrane (M), small membrane (sM) or haemagglutinin-esterase (HE) proteins. Only target cells expressing the virus spike (S) protein were recognized. Furthermore, the majority of CTL activity was restricted to target cells expressing the MHC class I D b molecules. Analysis of truncations and deletions of the S protein expressed by recombinant vaccinia viruses and peptide coated targets identified a single antigenic epitope, aa 510-518, conforming to the D b binding motif. These amino acids are contained within a domain deleted from a number of strains of mouse hepatitis virus, suggesting a role for immune pressure. To determine the potential for CTL specific for an epitope(s) within a non-structural protein, 24 CTL lines were established and characterized. No evidence for the induction of non-specific CTL activity or virus-specific CTL restricted to an epitope in a non-structural protein was obtained. These data indicate that the predominant CTL activity in JHMV-infected C57BL/6 mice is D b restricted and specific for a single epitope contained within aa 510-518 of the S protein.

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Protection from mouse hepatitis virus type 3-induced acute disease by an anti-nucleoprotein monoclonal antibody

Cited by 63 publications

References 17 publications

The M Protein of SARS-CoV: Basic Structural and Immunological Properties

The M Protein of SARS-CoV: Basic Structural and Immunological Properties

Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vectors protect mice against a lethal infection

The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response

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