Antibody to the 32K Structural Protein of Infectious Bursal Disease Virus Neutralizes Viral Infectivity in vitro and Confers Protection on Young Chickens

Fahey, K. J.; O’Donnell, Ian; Bagust, T. J.

doi:10.1099/0022-1317-66-12-2693

Cited by 38 publications

(14 citation statements)

References 14 publications

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“…These results confirm previous observations of the ability of VPX and VP2 to neutralize IBDV (1, 2, 4, 9, 24) and also show that the conformational neutralizing epitopes are present in recombinant VPX, as was expected due to the similar structure of the capsomers. However, they disagree with some previous data on the neutralizing ability of VP3 (6,21,26). Regarding the antigenicity, the dose required for coating the ELISA plates is similar to or lower than the antigen concentration using whole virus, confirming recombinant VPX's good antigenicity and suitability as a diagnostic tool.…”

Section: Discussioncontrasting

confidence: 54%

Antigenic Properties and Diagnostic Potential of Baculovirus-Expressed Infectious Bursal Disease Virus Proteins VPX and VP3

Martı́nez-Torrecuadrada

Lázaro

Rodrı́guez

et al. 2000

Clin Diagn Lab Immunol

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The routine technique for detecting antibodies specific to infectious bursal disease virus (IBDV) is a serological evaluation by enzyme-linked immunosorbent assay (ELISA) with preparations of whole virions as the antigens. To avoid using complete virus in the standard technique, we have developed two new antigens through the expression of the VPX and VP3 genes in insect cells. VPX and especially VP3 were expressed at high levels in insect cells and simple to purify. The immunogenicity of both proteins was similar to that of the native virus. VPX was able to elicit neutralizing antibodies but VP3 was not. Purified VPX and VP3 were tested in an indirect ELISA with more than 300 chicken sera. There was an excellent correlation between the results of the ELISA using VPX and those of the two commercial kits. VP3 did not perform as well as VPX, and the linear correlation was significantly lower. A comparison with the standard reference technique, seroneutralization, showed that the indirect ELISA was more sensitive. Therefore, VPX-based ELISA is a good alternative to conventional ELISAs that use whole virions.Infectious bursal disease (IBD), also called Gumboro disease, is a highly contagious viral disease. It causes heavy economic losses to the poultry industry worldwide, either by causing a high-mortality acute condition or by leading to immunosuppression in young chickens (between 3 and 6 weeks of age) provoked by the destruction of immature B lymphocytes within the bursa of Fabricius (14). IBD virus (IBDV) is the etiological agent of IBD. It belongs to the genus Avibirnavirus of the family Birnaviridae (20). To date, two antigenically distinct serotypes (I and II) of IBDV have been identified (12). Serotype I infects chickens and comprises at least six different subtypes of IBDV, which vary considerably in virulence (10). Viruses in one of these subtypes are routinely known as variant strains, whereas viruses in the other subtypes are known as classic strains. Serotype II infects mainly turkeys and is not pathogenic for chickens (12).The IBDV genome consists of two segments of doublestranded RNA designated A and B (3). Segment A encodes a 108-kDa polyprotein that is self-cleaved to produce VPX (48 kDa), VP3 (32 kDa), and VP4 (28 kDa). In the mature virions, VPX is processed into VP2 (41 kDa). VP2 and VP3 are the major structural proteins of the IBDV virion. VP2 has been identified as the main host-protective antigen of IBDV and carries major neutralizing epitopes (1, 2, 4, 23). VP3 is considered a group-specific antigen (2), and monoclonal antibodies directed to VP3 were able to prevent virus attachment (24) and to neutralize the virus (26). However, recombinant VP3 failed to protect chickens from challenge by virulent IBDV (21). Also, VP3 has been suggested to be the major immunogenic protein of IBDV, since the earliest antibodies that appear after infection with live or inactivated viruses are directed to VP3 (5).IBDV infection in young chickens is controlled by the transfer via yolk sac of maternal antibodies i...

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Section: Discussioncontrasting

confidence: 54%

Antigenic Properties and Diagnostic Potential of Baculovirus-Expressed Infectious Bursal Disease Virus Proteins VPX and VP3

Martı́nez-Torrecuadrada

Lázaro

Rodrı́guez

et al. 2000

Clin Diagn Lab Immunol

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“…The sequences of the other proteins are completely different (Miiller & Becht, 1982;Dobos, 1979). In addition, both VPX and VP2 react with the same MAb on Western blots (Fahey et al, 1985b;Becht et al, 1988). These observations suggest that VP2 is a specific cleavage product of a VPX precursor.…”

Section: Ibd V Genome Coding Assignmentsmentioning

confidence: 62%

Biochemistry and Immunology of Infectious Bursal Disease Virus

Kibenge

Dhillon

Russell

1988

Journal of General Virology

275

127

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“…There have been conflicting reports about the role played by the second major structural protein VP3 (Mr 32K) in the induction of neutralizing antibodies (Fahey et al, 1985;Azad et al, 1986); however, there is general agreement now that a conformation-dependent epitope located on VP2 represents the immunodominant determinant (Azad et al, 1987;Becht et al, 1988;Fahey et al, 1989). Binding of neutralizing monoclonal antibodies (MAbs) to fusion proteins produced by expression systems carrying stepwise truncated VP2 genes indicated that the genetic information for this antigenic domain is located in the central region of the VP2 gene (Azad et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

The genetic basis for the antigenicity of the VP2 protein of the infectious bursal disease virus

Schnitzler

Bernstein

Müller

et al. 1993

Journal of General Virology

111

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The genomic region coding for the antigenic structure responsible for the induction of neutralizing antibodies was localized in the central variable region of the VP2 gene by comparing the nucleotide sequence of five escape mutants derived from the standard infectious bursal disease virus strain Cu-1. Exchange of a single amino acid at one of the prominent hydrophilic parts of this region proved to be sufficient for altering the neutralizing properties. The reactivity of neutralizing antibodies with peptides expressed in vitro encompassing both hydrophilic areas suggests that the entire variable region is engaged in the formation of this conformationdependent antigenic site. VP2-specific, non-neutralizing monoclonal antibodies directed against the sequencedependent epitope of the serotype I strain Cu-1 and the serotype II strain 23/82 cross-reacted with peptides located towards the carboxy terminus of VP2; no reaction occurred with peptides derived from the aminoterminal side adjacent to the variable region.

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Antibody to the 32K Structural Protein of Infectious Bursal Disease Virus Neutralizes Viral Infectivity in vitro and Confers Protection on Young Chickens

Cited by 38 publications

References 14 publications

Antigenic Properties and Diagnostic Potential of Baculovirus-Expressed Infectious Bursal Disease Virus Proteins VPX and VP3

Antigenic Properties and Diagnostic Potential of Baculovirus-Expressed Infectious Bursal Disease Virus Proteins VPX and VP3

Biochemistry and Immunology of Infectious Bursal Disease Virus

The genetic basis for the antigenicity of the VP2 protein of the infectious bursal disease virus

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