scholarly journals Enzyme-labelled immunosorbent assay techniques in foot-and-mouth disease virus research

1978 ◽  
Vol 80 (3) ◽  
pp. 391-399 ◽  
Author(s):  
E. M. E. Abu Elzein ◽  
J. R. Crowther

SummaryThe indirect ELISA technique has been developed successfully to measure antibodies to foot-and-mouth disease virus (FMDV) in cattle sera. Preliminary studies using a standard serum assay show that reproducible results are obtained. The method should prove useful for the examination of antibody titres in sera from large numbers of cattle or other animals.

2021 ◽  
Author(s):  
Lucy Gordon ◽  
Neil Mabbott ◽  
Joanna Wells ◽  
Liudmila Kulik ◽  
Nick Juleff ◽  
...  

AbstractPrevious studies have shown after the resolution of acute infection and viraemia, foot- and-mouth disease virus (FMDV) capsid proteins and/or genome are localised in the light zone of germinal centres of lymphoid tissue in cattle and African buffalo. The pattern of staining for FMDV proteins was consistent with the virus binding to follicular dendritic cells (FDCs). We have now demonstrated a similar pattern of FMDV protein staining in mouse spleens after acute infection and showed FMDV proteins are colocalised with FDCs. Blocking antigen binding to complement receptor type 2 and 1 (CR2/CR1) prior to infection with FMDV significantly reduced the detection of viral proteins on FDCs and FMDV genomic RNA in spleen samples. Blocking the receptors prior to infection also significantly reduced neutralising antibody titres. Therefore, the binding of FMDV to FDCs and sustained induction of neutralising antibody responses are dependent on FMDV binding to CR2/CR1 in mice.Author SummaryFoot and mouth disease virus causes a highly contagious acute vesicular disease, resulting in more than 50% of cattle, regardless of vaccination status, and almost 100% of African buffalo becoming persistently infected for long periods (months) of time. Yet, the mechanisms associated with establishment of persistent infections are still poorly understood. Infected animals are characterised by the presence of long-lived neutralising antibody titres, which contrast with the short-lived response induced by vaccination. We have used a mouse model to understand how foot and mouth disease virus is trapped and retained in the spleen for up to 28 days post infection and how the absence of antigen in the germinal centre prevents a sustainable neutralising antibody response, in the mouse. Our results highlight the importance of targeting antigen to FDCs to stimulate potent neutralising antibody responses after vaccination.


2007 ◽  
Vol 88 (2) ◽  
pp. 487-492 ◽  
Author(s):  
A. L. Jackson ◽  
H. O'Neill ◽  
F. Maree ◽  
B. Blignaut ◽  
C. Carrillo ◽  
...  

The results of a simple pairwise-scanning analysis designed to identify inter-serotype recombination fragments, applied to genome data from 156 isolates of Foot-and-mouth disease virus (FMDV) representing all seven serotypes, are reported. Large numbers of candidate recombinant fragments were identified from all parts of the FMDV genome, with the exception of the capsid genes, within which such fragments are infrequent. As expected, intertypic fragment exchange is most common between geographically sympatric FMDV serotypes. After accounting for the likelihood of intertypic convergence in highly conserved parts of the FMDV genome, it is concluded that intertypic recombination is probably widespread throughout the non-structural genes, but that recombination over the 2B/C and 3B/C gene boundaries appears to be less frequent than expected, given the large numbers of recombinant gene fragments arising in these genes.


Author(s):  
S. S. Breese ◽  
H. L. Bachrach

Models for the structure of foot-and-mouth disease virus (FMDV) have been proposed from chemical and physical measurements (Brown, et al., 1970; Talbot and Brown, 1972; Strohmaier and Adam, 1976) and from rotational image-enhancement electron microscopy (Breese, et al., 1965). In this report we examine the surface structure of FMDV particles by high resolution electron microscopy and compare it with that of particles in which the outermost capsid protein VP3 (ca. 30, 000 daltons) has been split into smaller segments, two of which VP3a and VP3b have molecular weights of about 15, 000 daltons (Bachrach, et al., 1975).Highly purified and concentrated type A12, strain 119 FMDV (5 mg/ml) was prepared as previously described (Bachrach, et al., 1964) and stored at 4°C in 0. 2 M KC1-0. 5 M potassium phosphate buffer at pH 7. 5. For electron microscopy, 1. 0 ml samples of purified virus and trypsin-treated virus were dialyzed at 4°C against 0. 2 M NH4OAC at pH 7. 3, deposited onto carbonized formvar-coated copper screens and stained with phosphotungstic acid, pH 7. 3.


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