Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus.

Pfaff, Eberhard; Mussgay, M.; Böhm, H. O.; Schulz, Georg E.; Schaller, Heinz

doi:10.1002/j.1460-2075.1982.tb01262.x

Cited by 345 publications

(141 citation statements)

References 26 publications

Supporting

Mentioning

134

Contrasting

Order By: Relevance

“…Therefore, the most likely location of the neutralization epitope defined by MAb 12FE9* is between amino acids 138 and 143 or 145 and 162. The location of this neutralization epitope on FMDV O1 Campos VP 1 is similar to the location of neutralization epitopes on VP1 from FMDV O1 Kaufbeuren (Bittle et al, 1982;Pfaff et al, 1982;Strohmaier et al, 1982) and FMDV type A12 , suggesting that this area may have similar functions in different strains and types of FMDV.…”

Section: Discussionsupporting

confidence: 59%

Analysis of Foot-and-Mouth Disease Virus Type O1 Brugge Neutralization Epitopes Using Monoclonal Antibodies

Stave

Card

Morgan

1986

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYMonoclonal antibodies (MAbs) were elicited with inactivated, purified foot-andmouth disease virus (FMDV) type O1 strain Brugge (140S) and with 12S protein subunits. Each MAb was tested for its capacity to bind to FMDV O1 Brugge 140S virions, 12S subunits and purified VP1 by radioimmunoassay (RIA) and to neutralize viral infectivity in mouse protection assays. Those MAbs which reacted only with 12S subunits in RIA did not neutralize infectious virus. One MAb, 12FE9.2.1, reacted with 140S, 12S and purified VP 1 of FMDV O1 Brugge and neutralized infectious virus. Reactions with different biosynthetic FMDV type O1 Campos VP1 polypeptides localized the binding site of 12FE9.2.1 between amino acid residues 135 and 172. Eight MAbs reacted with both 140S virions and 12S subunits and neutralized infectious virus. Monoclonal antibodies that reacted only with 12S protein subunits or with 140S, 12S and VP1 did not compete in RIA with 140S/12S-reactive neutralizing MAbs for 12S binding sites. The ability of 140S/12S-reactive MAbs to compete for the 12S binding site defined by MAb 10GA4.2.2 was directly related to their capacity to neutralize infectious virus, suggesting that these MAbs were all affecting a single neutralization site. In mouse protection and plaque reduction neutralization assays, 10GA4.2.2 and 12FE9.2.1 were equally effective in neutralizing the homologous FMDV type O1 Brugge, and in cross-neutralization assays both exhibited high titres against four additional strains of type O1 FMDV.

show abstract

Section: Discussionsupporting

confidence: 59%

Analysis of Foot-and-Mouth Disease Virus Type O1 Brugge Neutralization Epitopes Using Monoclonal Antibodies

Stave

Card

Morgan

1986

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…The peptide obtained (~999, 1 mg) was conjugated with keyhole limpet hemocyanin [23]. Rabbits were immunized by a 2-fold subcutaneous injection of the conjugate (500 pg) with a 2-week interval.…”

Section: Methodsmentioning

confidence: 99%

Topology of Na⁺,K⁺‐ATPase Identification of the extra‐ and intracellular hydrophilic loops of the catalytic subunit by specific antibodies

et al. 1988

View full text Add to dashboard Cite

To study the topology of Na+,K+‐ATPase monoclonal antibodies (MAbs) specific for membrane‐bound enzyme were produced. Using immunofluorescence staining of viable cells or smears of a pig kidney embryonic (PKE) cell line, two groups of MAbs were selected, namely those binding to extra‐ or intracellular portions of the α‐subunit. The extracellular location of peptide loop 804–841 linking the Vth and VIth intramembrane hydrophobic segments was proved using MAb VG2. Another MAb, IIC9, interacting with PKE cells only after membrane perforation (4% formaldehyde and 0.1% Tween‐20), was shown to bind to the hydrophilic loop 868–945. The antigenic determinants recognized by MAb IIC9 and VG2 are located in peptides 887–904 and 810–825, respectively. The C‐terminus of the α‐subunit molecule was positioned on the outer side of the cytoplasmic membrane utilizing affinity‐purified antibodies to the synthetic peptide corresponding to fragment 999–1008.

show abstract

“…Antiviral responses to peptide immunogens have been extremely variable. The greatest progress has probably been achieved using peptides corresponding to the surface-exposed G-H loop of VP1 of foot-and-mouth disease virus (FMDV), which can elicit a neutralizing antibody response (Bittle et al, 1982;Pfaff et al, 1982) that is protective in target species (DiMarchi et al, 1986). Approximately 35 % of the antibodies induced by these peptides in laboratory animals also recognize virus (Parry et al, 1988) but, even so, the levels of protection attained in target species have been inconsistent.…”

Section: Introductionmentioning

confidence: 99%

Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2

Barnett

Rowlands

Parry

1993

Journal of General Virology

View full text Add to dashboard Cite

Synthetic peptides incorporating the derived amino acid sequence of VP2 residues 156 to 170 of human rhinovirus type 2 (HRV2) have previously been shown to elicit antibodies that neutralize virus infectivity. The proportion of virus-reactive antibodies present in polyclonal antisera to these peptides is, however, very low. Moreover, neutralization titrations of such antisera correlate poorly with other assays of either anti-virus or anti-peptide activity, suggesting the presence of antibodies with different specificities. To investigate these findings further, we produced a panel of monoclonal antibodies (MAbs) to VP2 peptides of residues 156 to 170 and characterized their reactions with a range of antigens in ELISA, precipitation and neutralization titrations. All the MAbs obtained recognized the homologous peptide, but could be divided into four main reaction groups according to their specificity for viral antigens. Antibodies in the first group recognized and neutralized native virus, apparently by preventing attachment to cells. A second group of MAbs bound to intact particles with similar affinities to the first group, but failed to neutralize infectivity. Antibodies in the third group recognized virus only after capsid distortions incurred by heating or by previous reaction with polyclonal antibodies. The fourth group comprised MAbs that were mainly peptide-specific. Some possible applications of anti-peptide MAbs to improving the design of peptide immunogens are considered.

show abstract

Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus.

Cited by 345 publications

References 26 publications

Analysis of Foot-and-Mouth Disease Virus Type O1 Brugge Neutralization Epitopes Using Monoclonal Antibodies

Analysis of Foot-and-Mouth Disease Virus Type O1 Brugge Neutralization Epitopes Using Monoclonal Antibodies

Topology of Na⁺,K⁺‐ATPase Identification of the extra‐ and intracellular hydrophilic loops of the catalytic subunit by specific antibodies

Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2

Contact Info

Product

Resources

About

Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus.

Cited by 345 publications

References 26 publications

Analysis of Foot-and-Mouth Disease Virus Type O1 Brugge Neutralization Epitopes Using Monoclonal Antibodies

Analysis of Foot-and-Mouth Disease Virus Type O1 Brugge Neutralization Epitopes Using Monoclonal Antibodies

Topology of Na+,K+‐ATPase Identification of the extra‐ and intracellular hydrophilic loops of the catalytic subunit by specific antibodies

Characterization of monoclonal antibodies raised against a synthetic peptide capable of inducing a neutralizing response to human rhinovirus type 2

Contact Info

Product

Resources

About

Topology of Na⁺,K⁺‐ATPase Identification of the extra‐ and intracellular hydrophilic loops of the catalytic subunit by specific antibodies