Fusion of bovine leukemia virus with target cells monitored by R18 fluorescence and PCR assays

Zarkik, Sarra; Defrise-Quertain, Fabienne; Portetelle, Daniel; Burny, Arsène; Ruysschaert, J. M.

doi:10.1128/jvi.71.1.738-740.1997

Cited by 7 publications

(4 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The results of antibody detection by SIIA revealed that colostrum from infected cattle inhibited syncytium induction caused by BLV infection. Syncytium formation results from cell-to-cell fusion caused by BLV gp51, an outer membrane glycoprotein [12, 13]. Previous studies showed the complement-dependent cytotoxicity of anti-gp51 antibody [14, 15], and previous studies hypothesized that the protective effect of BLV infection mediated by immunoglobulin (Ig) G would be conferred by anti-glycoprotein antibodies [16].…”

Section: Discussionmentioning

confidence: 99%

The effectiveness of colostral antibodies for preventing bovine leukemia virus (BLV) infection in vitro

et al. 2018

View full text Add to dashboard Cite

BackgroundBovine leukemia virus (BLV) is the causative agent of enzootic bovine leukosis (EBL). The incidence of EBL in Japan is increasing annually; and the cases of EBL in cattle younger than 2 years old has been reported. Therefore, it is vital to find a method to control BLV infection, especially in young calves. In this study, to evaluate the protective ability of colostral antibodies against BLV infection, as well as the potential for BLV infection mediated by colostrum/milk, we investigated temporal fluctuations in the anti-BLV antibody titer and BLV proviral load (PVL) in colostrum/milk and peripheral blood of six infected dams during lactation. The association between PVL and antibody titer in colostrum and peripheral blood was then investigated using samples from a further twenty-seven cattle. Antibody concentrations were measured with a Syncytium-induction Inhibition Assay using colostral/milk whey and serum. PVL in peripheral blood and colostrum was measured by real-time PCR.ResultsColostral antibodies showed high inhibitory activity until day 3 of lactation. The antibody titer and PVL in peripheral blood showed lesser changes than those in colostrum/milk throughout lactation. The colostral antibody titer was significantly higher than the serum antibody titer in all samples, whereas the colostrum PVL was significantly lower than the blood PVL. The blood PVL showed a significant correlation with serum antibody titer, colostrum PVL, and colostral antibody titer. However, there were no major correlations between the serum and colostral antibody titers.ConclusionsThis is the first report investigating the temporal changes in colostral antibody titer in terms of inhibiting BLV infection in vitro. The results of antibody detection by Syncytium-induction Inhibition Assay suggested that the protective activity of the colostral antibodies against BLV infection would be conferred by anti-BLV gp51 antibody. The high antibody titer of colostral whey suggests that colostral whey could be a potential source of antibodies with a low risk of infection in neonatal calves.

show abstract

Section: Discussionmentioning

confidence: 99%

The effectiveness of colostral antibodies for preventing bovine leukemia virus (BLV) infection in vitro

et al. 2018

View full text Add to dashboard Cite

show abstract

“…The first technique is testing the effects of agents, such as bafilomycin, that inhibit endosomal acidification. In some studies of this type, fusion has been measured directly by assessing the transfer of fluorescent probes from the virus to the target cell (Earp et al 2003;Irurzun et al 1997;Zarkik et al 1997). In others, fusion has been inferred by monitoring postfusion events, such as the synthesis of viral DNA (Mothes et al 2000).…”

Section: Low Ph Activationmentioning

confidence: 99%

The Many Mechanisms of Viral Membrane Fusion Proteins

Earp

Delos

Park

et al. 2004

Current Topics in Microbiology and Immunology

300

354

View full text Add to dashboard Cite

Every enveloped virus fuses its membrane with a host cell membrane, thereby releasing its genome into the cytoplasm and initiating the viral replication cycle. In each case, one or a small set of viral surface transmembrane glycoproteins mediates fusion. Viral fusion proteins vary in their mode of activation and in structural class. These features combine to yield many different fusion mechanisms. Despite their differences, common principles for how fusion proteins function are emerging: In response to an activating trigger, the metastable fusion protein converts to an extended, in some cases rodlike structure, which inserts into the target membrane via its fusion peptide. A subsequent conformational change causes the fusion protein to fold back upon itself, thereby bringing its fusion peptide and its transmembrane domain-and their attached target and viral membranes-into intimate contact. Fusion ensues as the initial lipid stalk progresses through local hemifusion, and then opening and enlargement of a fusion pore. Here we review recent advances in our understanding of how fusion proteins are activated, how fusion proteins change conformation during fusion, and what is happening to the lipids during fusion. We also briefly discuss the therapeutic potential of fusion inhibitors in treating viral infections.

show abstract

“…Моноклональные антитела против эпитопа H способны полностью блокировать слияние клеток в культуре. Антитела против эпитопов F и G менее эффективно снижают способность вируса к формированию синцития [27]. Помимо гуморального иммунитета, поверхностная субъединица также стимулирует Т-клеточный ответ, что продемонстрировано наличием хелперов CD4+ и эпитопов для цитотоксических CD8+ Т-лимфоцитов (CTL).…”

Section: организация генома вируса Blvunclassified

Structural characteristics of the bovine leukemia virus genome: A mini review

Fomenko

2023

Food systems

View full text Add to dashboard Cite

Enzootic bovine leukemia is an infectious disease with a chronic course caused by an RNA‑containing virus of the genus Deltaretrovirus. Despite the implementation of various programs for the elimination of leukemia, the disease is still widespread on the planet and continues to cause significant economic damage. A large proportion of BLV‑infected cattle remain to be asymptomatic carriers of the virus, which complicates diagnosis and contributes to the spread of the disease in the herd. The structure of the BLV genome is generally typical of retroviruses. It consists of genes encoding structural proteins, viral enzymes and regulatory elements flanked on both sides by identical long terminal repeats. The enzyme and structural protein coding genes (gag, pro, pol, and env) play a crucial role in the life cycle of the virus, influencing its infectivity and virion production. The tax and rex regulatory genes regulate viral transcription, export of transcripts from the nucleus to the cytoplasm, and disease progression. The increase in the number of copies of proviral DNA occurs mainly not due to the functioning of the virus reverse transcriptase, but because of clonal reproduction of the affected subpopulations of B‑cells, mainly CD5+ IgM+. This feature provides increased genetic stability of the BLV virus. These properties of the viral genome allow the development of a variety of PCR test systems. The widespread implementation of such systems enables the detection of carriers of the disease at early stages, which should contribute to the effective implementation of national programs to eradicate bovine leukemia.

show abstract

Fusion of bovine leukemia virus with target cells monitored by R18 fluorescence and PCR assays

Cited by 7 publications

References 28 publications

The effectiveness of colostral antibodies for preventing bovine leukemia virus (BLV) infection in vitro

The effectiveness of colostral antibodies for preventing bovine leukemia virus (BLV) infection in vitro

The Many Mechanisms of Viral Membrane Fusion Proteins

Structural characteristics of the bovine leukemia virus genome: A mini review

Contact Info

Product

Resources

About