Correlation of conformation and biological activity in lysozyme “loop” homologs

Arnon, Ruth; Teicher, Edna; Scheraga, Harold A.

doi:10.1016/0022-2836(74)90382-9

Cited by 18 publications

(3 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…According to these authors, only three antigenic sites exist in lysozyme, and all of these sites are "discontinuous". However, evidence was reported from several other laboratories that additional antigenic regions might exist in a lysozyme molecule (Maron et al, 1972;Sakato et al, 1972;Arnon et al, 1974;Fainaru et al, 1974;Matthyssens et al, 1974;Fujio et al, 1974;Wilson & Prager, 1974;Ibrahimi et al, 1979).…”

mentioning

confidence: 92%

Antibodies to a continuous region at residues 38-54 of hen egg white lysozyme found in a small fraction of anti-hen egg white lysozyme antibodies

Tsutsumi¹,

Hirayama²,

Fujio³

et al. 1980

Biochemistry

View full text Add to dashboard Cite

The antigenic reactivity of the region at residues 38-54 of hen egg white lysozyme (lysozyme) was investigated by using various rabbit, goat, and sheep anti-lysozyme antisera by the charcoal-dextran method. This continuous antigenic region was completely independent in its specificity from other discontinuous antigenic regions of lysozyme. The antibodies to this region were shown to be reactive with native lysozyme as well as thermolytic nondisulfide peptides (residues 38-54 and 38-57) and synthetic peptides (sequences 38-48 and 34-54) by the following evidence. (1) The antigen binding activity could be inhibited by the addition of native lysozyme.(2) The antibodies to this region could be absorbed with lysozyme immunoadsorbent. (3) The specific antibodies prepared by the synthetic peptide (sequence 38-48) immunoad-

show abstract

mentioning

confidence: 92%

Antibodies to a continuous region at residues 38-54 of hen egg white lysozyme found in a small fraction of anti-hen egg white lysozyme antibodies

Tsutsumi¹,

Hirayama²,

Fujio³

et al. 1980

Biochemistry

View full text Add to dashboard Cite

show abstract

“…Norleucine has the same overall shape as methionine (Barany & Merrifield, 1980) and, of all possible alternative amino acids, alanine has the most similar overall shape as cysteine. This substitution was also applied in other studies (Arnon et aL, 1974;Jacob et al, 1983). The peptides were desalted and the N-terminal amino acid was determined by dansylation (Wootton et aL, 1975).…”

Section: Methodsmentioning

confidence: 99%

Virus Neutralizing Activity Induced by Synthetic Peptides of Glycoprotein D of Herpes Simplex Virus Type 1, selected by their Reactivity with Hyperimmune Sera from Mice

Geerligs

Kocken

Drijfhout

et al. 1990

Journal of General Virology

View full text Add to dashboard Cite

Mice were immunized with synthetic peptides covering the first 56 amino acids of herpes simplex virus type 1 (HSV-1) glycoprotein D (gD) and a fusion protein, produced in Escheriehia coli, containing the first 55 amino acid residues of gD. It was found that mice immunized with peptides composed of amino acid residues 1 to 13, 18 to 30, 22 to 38 and 38 to 56 ofgD were not significantly protected against a lethal challenge with HSV-1. Immunization with peptide 9-21 and the gD fusion protein resulted in significant protection. Antisera, from mice immunized with HSV-I, were investigated for reactivity with a series of 57 overlapping gD peptides covering the entire amino acid sequence, except for the membrane-spanning region. All antisera reacted with peptides 9-21, 10-24, 151-165, 216-232, 282-301 and with peptide 340-354 located in the anchoring region of gD, and 15 other peptides were recognized by at least one antiserum. Twelve peptides (10-24, 151-165, 216-232, 244-267, 260-274, 270-284, 260-284, 282-301,300-314, 340-354, 348-362 and 355-369) reacted most frequently with the hyperimmune sera from mice and were selected for further study. These were conjugated to bovine serum albumin and used to immunize rabbits. Only antisera against peptide 10-24, which covers the same epitope as peptide 9-21, neutralized HSV-1 in vitro.

show abstract

“…The peptides, each consisting of 15 amino acids, were synthesized by the method of Houghten [10] , and cysteine at positions 66, 106, 118, 127, 189, and 202 were substituted by norleucine or alanine, respectively. Norleucine has the same overall shape as methionine [2] and of all possible, alternative amino acids, atanine has the most similar overall shape as cysteine [1,12]. The peptides were desalted and the N-terminal amino acid was determined by dansylation [18].…”

Section: Summary Thirty Eight Human Sera Seropositive For Herpes Simentioning

confidence: 99%

Reactivity of human sera with overlapping synthetic peptides of herpes simplex virus type 1 glycoprotein D

Geerligs

Feijlbrief

Bolk

et al. 1990

Archives of Virology

View full text Add to dashboard Cite

Thirty eight human sera, seropositive for herpes simplex virus (HSV) and 56 human sera, seronegative for HSV by immunofluorescence and by ELISA, were investigated for reactivity with a series of overlapping synthetic peptides of HSV type 1 glycoprotein D (gD-1). Thirty four out of the 38 human sera positive for HSV reacted with peptides located between residues 300 and 369; the HSV-negative sera reacted with six of the gD-1 peptides, but with none of the peptides within residues 300 to 369.

show abstract

Correlation of conformation and biological activity in lysozyme “loop” homologs

Cited by 18 publications

References 7 publications

Antibodies to a continuous region at residues 38-54 of hen egg white lysozyme found in a small fraction of anti-hen egg white lysozyme antibodies

Antibodies to a continuous region at residues 38-54 of hen egg white lysozyme found in a small fraction of anti-hen egg white lysozyme antibodies

Virus Neutralizing Activity Induced by Synthetic Peptides of Glycoprotein D of Herpes Simplex Virus Type 1, selected by their Reactivity with Hyperimmune Sera from Mice

Reactivity of human sera with overlapping synthetic peptides of herpes simplex virus type 1 glycoprotein D

Contact Info

Product

Resources

About