Identification of a major antibody binding epitope in the non-structural protein 3D of foot-and-mouth disease virus in cattle and the development of a monoclonal antibody with diagnostic applications

Yang, Ming; Clavijo, Alfonso; Li, Mingyi; Hole, Kate; Holland, H.; Wang, He; Deng, Ming

doi:10.1016/j.jim.2007.01.016

Cited by 41 publications

(33 citation statements)

References 25 publications

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“…Mouse anti-human ␤ 6 (MAB2076Z; Chemicon) was used to detect the bovine integrin subunit ␤ 6 at a 1:300 dilution. The mouse monoclonal antibody F19-51 (20) was used to detect the FMDV 3D protein at a 1:200 dilution.…”

Section: Methodsmentioning

confidence: 99%

A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine α_Vβ₆Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus

LaRocco

Krug

Kramer³

et al. 2013

J Clin Microbiol

133

113

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Foot-and-mouth disease (FMD) is a worldwide problem limiting the trade of animals and their products from affected countries. The rapid isolation, serotyping, and vaccine matching of FMD virus from disease outbreaks is critical for enabling the implementation of effective vaccination programs and to stop the spread of infection during outbreaks. Some primary cells have been shown to be highly susceptible to most strains of FMD virus (FMDV) but are difficult and expensive to prepare and maintain. Since the ␣ V ␤ 6 integrin is a principal receptor for FMDV, we transduced a bovine kidney cell line to stably express both the ␣ V and ␤ 6 bovine integrin subunits. This stable cell line (LFBK-␣ V ␤ 6 ) showed ␤ 6 expression and enhanced susceptibility to FMDV infection for >100 cell passages. LFBK-␣ V ␤ 6 cells were highly sensitive for detecting all serotypes of FMDV from experimentally infected animals, including the porcinophilic FMDV strain O/TAW/97. In comparison to other cell types that are currently used for virus isolation, LFBK-␣ V ␤ 6 cells were more effective at detecting FMDV in clinical samples, supporting their use as a more sensitive tool for virus isolation.F oot-and-mouth disease virus (FMDV) is a severe economic concern for meat-producing nations since the trade of animal products is limited in the countries where the virus is present. The rapid spread of the virus among susceptible animals results in severe morbidity and, in some cases, death, especially in young animals (reviewed in reference 1). Infection or vaccination with one of the seven different serotypes does not confer cross-protection to other serotypes or even to some subtypes of the same serotype. Vaccines for FMDV are widely used to prevent clinical disease, but since vaccines are serotype and subtype specific, the virus(es) causing outbreaks must be isolated and serologically characterized for vaccine matching prior to selecting the appropriate vaccine antigen to be used in vaccine formulations (reviewed in reference 2).Although molecular techniques, such as PCR coupled with genomic sequencing, can be used in samples containing enough virus to rapidly identify the virus serotype and its relationship to other FMDV strains, appropriate vaccine prediction requires virus growth in cell culture to carry out neutralization tests using reference sera. Inefficient recovery of virus from animal samples can delay diagnosis and vaccine selection, hampering the rapid implementation of control measures; thus, virus isolation protocols are designed for maximum sensitivity. Some primary cells, such as bovine thyroid (BTY), are highly susceptible to a wide range of FMDV serotypes (3), but they are difficult and costly to prepare and lose FMDV susceptibility after multiple passages (4). Primary lamb kidney (LK) cells are also very sensitive to FMDV, and unlike BTY cells, LK cells maintain their sensitivity to FMDV infection after cryopreservation (5). Immortalized cell lines (e.g., baby hamster kidney fibroblasts and porcine kidney epithelial cells), ...

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Section: Methodsmentioning

confidence: 99%

A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine α_Vβ₆Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus

LaRocco

Krug

Kramer³

et al. 2013

J Clin Microbiol

133

113

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“…Comparison of the 3D pol sequences of FMDV and BRV-2 viruses revealed 64% identity (20) at the amino acid level. Amino acids 16 to 32 comprise an important antigenic site in the FMDV 3D pol protein (49), and this peptide is 76% identical between these two closely related viruses. MAbs F32-44 and F83B targeted against native FMDV 3D pol and 3B protein, respectively, showed high reactivity against A 24 WT protein but did not react with BRV-2.…”

Section: Discussionmentioning

confidence: 99%

“…The presence of a 3D pol marker in the vaccine candidate is particularly important since the FMDV 3D pol protein is known to stimulate a strong humoral response that is detectable early after infection and therefore is valuable in assessing infectious status during control of an outbreak (9,12). In the present study, we utilized a modified cELISA (49) to capture the 3D pol antigen to the solid phase, and the ability of test sera to inhibit the binding of the MAb F32-44 to the antigen was evaluated. Likewise, a similar in-house cELISA based on MAb F83B (targeted against 3B protein) was used to detect serological responses to the epitope contained in the 3B viral protein.…”

Section: Discussionmentioning

confidence: 99%

“…The MAbs used in the present study were the MAbs F19-2 and F32-44 directed against the FMDV 3D pol (49) and MAb F83B directed against the 3B nonstructural protein (19). Briefly, cell monolayers grown in 24-well plates were infected with A 24 WT, A 24 WT3D YR , A 24 LL, A 24 LL3D YR , A 24 WT3B PVKV 3D YR , or A 24 LL3B PVKV 3D YR at an MOI of 5.…”

Section: Methodsmentioning

confidence: 99%

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A Safe Foot-and-Mouth Disease Vaccine Platform with Two Negative Markers for Differentiating Infected from Vaccinated Animals

Uddowla

Hollister

Pacheco

et al. 2012

J Virol

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“…Different species may recognize different epitopes. Sera from FMDV-infected pigs failed to react with any linear epitope located on the 3D protein (35). The peptide used for immunization in this study was recognized by sera from all infected animals independently of the animal species (20).…”

Section: Discussionmentioning

confidence: 72%

Development of a Competitive Enzyme-Linked Immunosorbent Assay for Detection of Antibodies against the 3B Protein of Foot-and-Mouth Disease Virus

Yang¹,

Parida²,

Salo³

et al. 2015

Clin. Vaccine Immunol.

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Foot-and-mouth disease (FMD) is one of the most highly contagious and economically devastating diseases, and it severely constrains the international trade of animals. Vaccination against FMD is a key element in the control of FMD. However, vaccination of susceptible animals raises critical issues, such as the differentiation of infected animals from vaccinated animals. The current study developed a reliable and rapid test to detect antibodies against the conserved, nonstructural proteins (NSPs) of the FMD virus (FMDV) to distinguish infected animals from vaccinated animals. A monoclonal antibody (MAb) against the FMDV NSP 3B was produced. A competitive enzyme-linked immunosorbent assay (cELISA) for FMDV/NSP antibody detection was developed using a recombinant 3ABC protein as the antigen and the 3B-specific MAb. Sera collected from naive, FMDV experimentally infected, vaccinated carrier, and noncarrier animals were tested using the 3B cELISA. The diagnostic specificity was 99.4% for naive animals (cattle, pigs, and sheep) and 99.7% for vaccinated noncarrier animals. The diagnostic sensitivity was 100% for experimentally inoculated animals and 64% for vaccinated carrier animals. The performance of this 3B cELISA was compared to that of four commercial ELISA kits using a panel of serum samples established by the World Reference Laboratory for FMD at The Pirbright Institute, Pirbright, United Kingdom. The diagnostic sensitivity of the 3B cELISA for the panel of FMDV/NSP-positive bovine serum samples was 94%, which was comparable to or better than that of the commercially available NSP antibody detection kits. This 3B cELISA is a simple, reliable test to detect antibodies against FMDV nonstructural proteins.

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Identification of a major antibody binding epitope in the non-structural protein 3D of foot-and-mouth disease virus in cattle and the development of a monoclonal antibody with diagnostic applications

Cited by 41 publications

References 25 publications

A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine α_Vβ₆Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus

A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine α_Vβ₆Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus

A Safe Foot-and-Mouth Disease Vaccine Platform with Two Negative Markers for Differentiating Infected from Vaccinated Animals

Development of a Competitive Enzyme-Linked Immunosorbent Assay for Detection of Antibodies against the 3B Protein of Foot-and-Mouth Disease Virus

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Identification of a major antibody binding epitope in the non-structural protein 3D of foot-and-mouth disease virus in cattle and the development of a monoclonal antibody with diagnostic applications

Cited by 41 publications

References 25 publications

A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine αVβ6Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus

A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine αVβ6Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus

A Safe Foot-and-Mouth Disease Vaccine Platform with Two Negative Markers for Differentiating Infected from Vaccinated Animals

Development of a Competitive Enzyme-Linked Immunosorbent Assay for Detection of Antibodies against the 3B Protein of Foot-and-Mouth Disease Virus

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Product

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A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine α_Vβ₆Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus

A Continuous Bovine Kidney Cell Line Constitutively Expressing Bovine α_Vβ₆Integrin Has Increased Susceptibility to Foot-and-Mouth Disease Virus