Elisa, A Highly Sensitive and Specific Method for Diagnosis of Bovine Leukemia Virus Infection

Portetelle, Daniel; Mammerickx, Marc

doi:10.1007/978-1-4613-2341-9_16

Cited by 4 publications

(4 citation statements)

References 26 publications

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“…They are characterized by their anti-gpSl antibody titers (21) and number of peripheral lymphocytes (per cubic millimeter): B78, 0 and 7,371; B68, 540 and 7,268; B71, 14,580 and 6,015; B73, 1,620 and 5,201; B79, 180 and 5,156; and B80, 540 and 5,156. Peptide synthesis; production and reactivity of rabbit antipeptide antibodies.…”

Section: Methodsmentioning

confidence: 99%

“…Antibody titers were assessed from the reactions of the antisera with their corresponding peptides (100 ng per well) in enzymelinked immunosorbent assays (ELISAs) and calculated as the reverse of the serum dilution for which the optical density is twice that of the preimmune serum. Titration of the antisera against the whole BLV particles disrupted with N-octylglucoside (19) or against gpSl presented by the MAb directed against site E (MAb E [21]) was also performed in ELISAs. Negative controls were performed with the rabbit sera before immunization.…”

Section: Methodsmentioning

confidence: 99%

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Mapping of B-neutralizing and T-helper cell epitopes on the bovine leukemia virus external glycoprotein gp51

Callebaut

Voneche

Mager

et al. 1993

J Virol

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A battery of 19 synthetic peptides was used to characterize efficient neutralizing and helper T-celi epitopes on the bovine leukemia virus (BLV) external envelope glycoprotein gp5l. Four of the antipeptide antisera raised in rabbits inhibited the formation of BLV-induced syncytia; these antisera are directed against peptides 64-73, 98-117, and 177-192. Only antisera directed against the 177-192 region also neutralized vesicular stomatis virus-BLV pseudotypes. This study clearly demonstrates that neutralizing properties can be observed with antibodies raised to regions undescribed so far and induded in both the amino-terminal and central parts of the antigen. In addition, some helper T-cell determinants were defined from gpSl-immunized mice and from BLV-infected cattle. Although none of the peptides tested behaved as a universal helper T-celi epitope, peptide 98-117 stimulated T-cell proliferation from BALB/c mice and from three infected cows, while peptide 169-188 strongly stimulated T-cell proliferation from one infected cow. Further experiments performed with three peptides overlapping the 169-188 region (177-192, 179-192, 181-192) demonstrated the particular relevance of residue(s) P-177 and/or D-178 in the helper T-celi epitope. These data should assist in the design of an efficient subunit vaccine against BLV infection that contains peptides possessing both B-neutralizing and helper T-cell determinants.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Mapping of B-neutralizing and T-helper cell epitopes on the bovine leukemia virus external glycoprotein gp51

Callebaut

Voneche

Mager

et al. 1993

J Virol

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“…Curiously enough, it has been demonstrated that one overlapping peptide (peptide 142 -161) contains the sequential site E, defined by a non-neutralizing mAb [37]. However, this site was previously suspected to be important for oligomerization since mAbE presents the external glycoprotein gp5 1 in a quasi-native configuration, as obtained with the total gp51-gp30 complex [38]. Furthermore, this site is relatively inaccessible on the complete oligomer [39].…”

Section: A L A~a P ---~H H a V S D H E A T L R C W A L S F Y -P A E -Bmentioning

confidence: 99%

Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data

Callebaut

Portetelle

Burny

et al. 1994

European Journal of Biochemistry

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Sequence analysis using the sensitive hydrophobic cluster analysis method shows that the bovine leukemia virus envelope glycoproteins conserve the general organization of the influenza hemagglutinin into a 'stem', containing the external part of the transmembrane glycoprotein and the Nterminal and C-terminal parts of the external glycoprotein, and a 'head', containing only external glycoprotein residues. However, our analysis suggests, for the first time, that the bovine leukemia virus envelope head will not adopt the typical 'jelly-roll' fold of the influenza A hemagglutinin head, but most likely folds into another type of 'Greek-key' structure corresponding to the overall topology of constant immunoglobulin domains. We constructed a three-dimensional model for the bovine leukemia virus envelope head by homology modeling using the crystal structure of the human histocompatibility antigen HLA-A2 a3 domain. Furthermore, we propose a general model for the oligomeric organization of this head, based on the hemagglutinin trimer. The proposed structural organization of bovine leukemia virus external glycoprotein is further supported by antipeptide and monoclonal antibody reactivities. Our modeling study suggests that the loops of the two neutralizing peptides located in the head are adjacent at the top of the domain and define a potential interaction site of the external glycoprotein with its cellular receptor. This site is topologically similar to the binding site of hemagglutinin with its cellular receptor, sialic acid. The other neutralizing peptides are located within a small domain linking the head to the stem.These data are of interest for defining other oncoviral glycoproteins heads and receptor-binding sites.

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“…Positive reactions were monitored with goatanti-rabbit immunoglobulins labeled with peroxydase (POD). Production and purification of BLV vihons were essentially as deschbed by Portetelle et al (1987).…”

Section: Enzyme-linked Immunosorbent Assays (Elisas)mentioning

confidence: 99%

Use of synthetic peptides to map sequential epitopes recognized by monoclonal antibodies on the bovine leukemia virus external glycoprotein

et al. 1991

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Six sequential epitopes (A, B, B', D, D', E) were previously defined on the bovine leukemia virus (BLV) envelope glycoprotein gp51 by their reactivity with monoclonal antibodies. A panel of synthetic peptides covering almost the entire sequence of gp51 was tested in enzyme-linked immunosorbent assays in order to localize these epitopes. E was shown to be included in peptide 142-161 (MCF4), B and B' in peptide 195-205, D and D' in peptide 218-237 (MCF6), and A in peptide 249-268 (MCF7). These results extend and confirm previous observations suggesting that the sequential epitopes recognized by our battery of monoclonal antibodies are located in the carboxylic half of BLV gp51.

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Elisa, A Highly Sensitive and Specific Method for Diagnosis of Bovine Leukemia Virus Infection

Cited by 4 publications

References 26 publications

Mapping of B-neutralizing and T-helper cell epitopes on the bovine leukemia virus external glycoprotein gp51

Mapping of B-neutralizing and T-helper cell epitopes on the bovine leukemia virus external glycoprotein gp51

Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data

Use of synthetic peptides to map sequential epitopes recognized by monoclonal antibodies on the bovine leukemia virus external glycoprotein

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