Monoclonal and Polyclonal Antibodies Specific for Foot and Mouth Disease Virus Type A and Type O VP1

Cho, Jin Gu; Jo, Yeong Joon; Sung, Jong Hwan; Hong, Jang Kwan; Hwang, Ji Hyeon; Park, Jong Hyeon; Lee, Kwang Nyeong; Park, Sang Gyu

doi:10.1089/hyb.2012.0034

Cited by 7 publications

(8 citation statements)

References 21 publications

(17 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…DAPI staining indicated that VP1 was mainly located in the cytoplasm of the infected cells ( Fig. 1A ), although some VP1 were detected in the nucleus, which is consistent with a previous report on the VP1 protein of FMDV [ 22 ]. The neutralizing activity of mAb 2D10 was then determined by use of an in vitro neutralization assay on DEF cells; mAb 2D10 neutralized the DHAV-1 HP1 virus with a neutralization titer (NT 50 ) of 40.…”

Section: Resultssupporting

confidence: 92%

Identification of a Conserved B-Cell Epitope on Duck Hepatitis A Type 1 Virus VP1 Protein

Zhang

et al. 2015

PLoS ONE

View full text Add to dashboard Cite

BackgroundThe VP1 protein of duck hepatitis A virus (DHAV) is a major structural protein that induces neutralizing antibodies in ducks; however, B-cell epitopes on the VP1 protein of duck hepatitis A genotype 1 virus (DHAV-1) have not been characterized.Methods and ResultsTo characterize B-cell epitopes on VP1, we used the monoclonal antibody (mAb) 2D10 against Escherichia coli-expressed VP1 of DHAV-1. In vitro, mAb 2D10 neutralized DHAV-1 virus. By using an array of overlapping 12-mer peptides, we found that mAb 2D10 recognized phages displaying peptides with the consensus motif LPAPTS. Sequence alignment showed that the epitope 173LPAPTS178 is highly conserved among the DHAV-1 genotypes. Moreover, the six amino acid peptide LPAPTS was proven to be the minimal unit of the epitope with maximal binding activity to mAb 2D10. DHAV-1–positive duck serum reacted with the epitope in dot blotting assay, revealing the importance of the six amino acids of the epitope for antibody-epitope binding. Competitive inhibition assays of mAb 2D10 binding to synthetic LPAPTS peptides and truncated VP1 protein fragments, detected by Western blotting, also verify that LPAPTS was the VP1 epitope.Conclusions and SignificanceWe identified LPAPTS as a VP1-specific linear B-cell epitope recognized by the neutralizing mAb 2D10. Our findings have potential applications in the development of diagnostic techniques and epitope-based marker vaccines against DHAV-1.

show abstract

Section: Resultssupporting

confidence: 92%

Identification of a Conserved B-Cell Epitope on Duck Hepatitis A Type 1 Virus VP1 Protein

Zhang

et al. 2015

PLoS ONE

View full text Add to dashboard Cite

show abstract

“…In response to a need for additional laboratory reagents to support the study of FMDV, new antibodies recognizing the NS protein 3AB (Lin et al., ), and VP1 of type A and type O (Cho et al., ) have recently been characterized. Furthermore, scientists at PIADC have developed a quantitative colorimetric bioassay to measure the anti‐FMDV activity of bovine and porcine type I IFNs (Ramanathan et al., ).…”

Section: Molecular Biologymentioning

confidence: 99%

Global Foot-and-Mouth Disease Research Update and Gap Analysis: 7 - Pathogenesis and Molecular Biology

Robinson

Knight-Jones

Charleston

et al. 2016

Transbound Emerg Dis

View full text Add to dashboard Cite

SummaryWe assessed research knowledge gaps in the fields of FMDV (foot-and-mouth disease virus) pathogenesis and molecular biology by performing a literature review and collecting research updates (2014) from 33 institutes from across the world. Findings were used to identify priority areas for future research. There have been important advances in FMDV pathogenesis; FMDV remains in lymph nodes of many recovered animals that otherwise do not appear persistently infected, even in species previously not associated with the carrier state. Whether virus retention helps maintain host immunity and/or virus survival is not known. Studies of FMDV pathogenesis in wildlife have provided insights into disease epidemiology, in endemic and epidemic settings. Many aspects of FMDV infection and virus entry remain unknown; however, at the cellular level, we know that expression level and availability of integrins (that permit viral entry), rate of clearance of infected cells and strength of anti-viral type I IFN (interferon) response are key determinants of tissue tropism. Extending findings to improved understanding of transmission requires a standardized approach and adoption of natural routes of infection during experimental study. There has been recognition of the importance of autophagosomes for FMDV entry into the cytoplasm following cell surface receptor binding, and that distinct internal cellular membranes are exploited for viral replication and immune evasion. New roles for viral proteins in blocking type I IFN production and downstream signalling have been identified facilitating research in anti-viral therapeutics. We know more about how infection affects cell protein expression, and research into molecular determinants of capsid stability has aided the development of stable vaccines. We have an expanding knowledge of viral and host molecular determinates of virulence and infectiousness, and of how phylogenetics may be used to estimate vaccine match and strain distribution. With ongoing advances, these areas could translate into significantly improved disease control.

show abstract

“…The expression of the med28 protein was induced by 0.1 mM IPTG at 30°C for 4 h. Protein purification method has been described previously. (11) The cells were harvested, resuspended in 1X PBS, and then lysed by ultrasonication. After centrifugation of the lysate at 8000 g, the pellet was recovered and further solubilized using 1X PBS containing 6 M guanidine-HCl.…”

Section: Generation Of Recombinant Med28 Proteinmentioning

confidence: 99%

“…Methods were followed as described previously. (11) To generate mouse monoclonal antibody, female BALB/C mice (13 weeks old) were immunized subcutaneously. The emulsion was produced by complete mixing of med28 protein (200 mg/200 mL) with equal volume of complete Freund adjuvant (Sigma-Aldrich, St. Louis, MO).…”

Section: Generation Of Monoclonal Antibodiesmentioning

confidence: 99%

See 1 more Smart Citation

Generation of Med28 Specific Monoclonal Antibodies

Cho

Kim³

et al. 2015

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy

Self Cite

View full text Add to dashboard Cite

1Med28 plays a role in transcription, signal transduction, and cell proliferation. The overexpression of med28 is associated with tumor progression in in vitro and in vivo models. Recently it has been reported that the elevated expression of med28 is associated with poor outcome in women with breast cancer. The expression level of med28 in in vitro and in vivo was examined by using anti-rabbit polyclonal antibody in previous reports. In this study, we report for the first time the generation and characterization of four monoclonal antibodies against med28 through immunoblotting, immunofluorescence microscopy, immunoprecipitation, and immunohistochemical analyses. These antibodies will be useful in detecting med28 in in vitro and in vivo.

show abstract

Monoclonal and Polyclonal Antibodies Specific for Foot and Mouth Disease Virus Type A and Type O VP1

Cited by 7 publications

References 21 publications

Identification of a Conserved B-Cell Epitope on Duck Hepatitis A Type 1 Virus VP1 Protein

Identification of a Conserved B-Cell Epitope on Duck Hepatitis A Type 1 Virus VP1 Protein

Global Foot-and-Mouth Disease Research Update and Gap Analysis: 7 - Pathogenesis and Molecular Biology

Generation of Med28 Specific Monoclonal Antibodies

Contact Info

Product

Resources

About