Localisation of a receptor‐recognition domain on the S3 subunit of pertussis toxin by peptide mapping

Tallett, April; Seabrook, R N; Irons, L.I.; Robinson, A.; Heyningen, Simon van; Atkinson, Tony

doi:10.1111/j.1432-1033.1993.tb17604.x

Cited by 5 publications

(3 citation statements)

References 35 publications

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“…The corresponding residue in the S2 subunit is a leucine, which also interacts with the conserved isoleucine residue. Other studies that point to a role for the APT domain in carbohydrate binding have used synthetic peptides or mutagenesis of the isolated S2 and S3 domains (Saukkonen et al ., 1992; Rozdzinski et al ., 1993; Tallett et al ., 1993; Heerze et al ., 1995).…”

Section: Discussionmentioning

confidence: 99%

Aerolysin and pertussis toxin share a common receptor-binding domain

et al. 1997

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We have discovered that the bacterial toxins aerolysin and pertussis toxin share a common domain. This is surprising because the two toxins affect cells in very different ways. The common domain, which we call the APT domain, consists of two three‐stranded antiparallel β‐sheets that come together and wrap around a central pair of helices. The APT domain shares a common fold with the C‐type lectins and Link modules, and there appears to be a divergent relationship among the three families. One surface region of the APT domain is highly conserved, raising the possibility that the domains have a common function in both proteins. Mutation of one of the conserved surface residues in aerolysin, Tyr61, results in reduced receptor binding and activity, thus providing evidence that the APT domain may be involved in interaction with the toxin's receptor. Structural and biochemical evidence suggests that the APT domain contains a carbohydrate‐binding site that can direct the toxins to their target cells.

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Section: Discussionmentioning

confidence: 99%

Aerolysin and pertussis toxin share a common receptor-binding domain

et al. 1997

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“…Localization of a receptor-recognition domain on the S3 cell adhesion subunit of pertussis toxin has been accomplished by peptide mapping against the glycoprotein fetuin. 25 The sequence RQITPGWSIY was shown to bind to fetuin.…”

Section: B Applicationsmentioning

confidence: 99%

Spatially Addressable Combinatorial Libraries

Pirrung

1997

Chem. Rev.

167

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ContentsI. Introduction 473 II. Peptides-on-Pins 474 A. Method 474 B. Applications 476 III. Macroscopic DNA Arrays 478 A. Method 478 B. Applications 479 IV. Light-Directed Synthesis 480 A. Background 480 B. Method 480 C. Applications 483 1. Peptides 483 2. DNA 484 V. Peptides on Paper 485 A. Method 485 B. Applications 486 VI. Inorganic Combinatorial Libraries 486 A. Method 486 B. Applications 487 VII. Conclusions 487 VIII. References and Notes 487Michael Pirrung (b. 1955) grew up in the rodeo capital of Texas, Mesquite. After graduating from the University of TexassAustin, he pursued a Ph.D. at UC-Berkeley. He did research on stereoselective aldol condensations with Clayton Heathcock and an independent project on a photochemical total synthesis of isocomene. After a postdoc with Gilbert Stork at Columbia, he took a position at Stanford. His group became known for work on the mechanism of the biosynthesis of ethylene, the plant-ripening hormone. In 1988, he joined a "working group" of scientists meeting in Palo Alto to form a then-new company, Affymax. He established the chemistry program at Affymax, focusing on methods of creating chemical diversity. His work there on light-directed synthesis was recognized with the AAAS-Newcomb Cleveland Prize. In 1990, he moved to Duke University where he is now Professor of Chemistry and Director of the Program in Biological Chemistry. He has published ∼100 peer-reviewed articles and holds several patents. A sabbatical at the Baylor College of Medicine in 1995 resulted in one current interest, chip-based comparison sequencing for mutation detection in highly mutated disease genes.Continuing interests include asymmetric catalysis, synthetic methodology, total synthesis, photochemistry, enzymology, combinatorial chemistry, lightdirected synthesis, and ethylene biosynthesis.

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“…Epitope mapping. Consecutive overlapping peptides, synthesized on polyethylene pins and corresponding, respectively, to the Fim2 and Fim3 major subunit amino acid sequences (Livey et al, 1987;Mooi e t al., 1990), were prepared using the protocol already described (Tallet et al, 1993). Both 10-and 8-residue peptides, overlapping by 5 and 6 residues, respectively, were synthesized for each subunit amino acid sequence.…”

Section: A M P E a R C E A N D O T H E R Smentioning

confidence: 99%

Localization of antigenic domains on the major subunits of Bordetella pertussis serotype 2 and 3 fimbriae

et al. 1994

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Antibody-binding domains on the major subunits of Bordetella pertussis serotype 2 (Fim2) and 3 fimbriae (Fim3) have been identified using synthetic peptides which were screened for recognition by anti-protein monoclonal antibodies (mAbs). The presence of non-contiguous f imbrial epitopes was demonstrated by both anti-Fim2 and anti-Fim3 mAbs, several of which recognized at least two peptides that were discontinuous in the amino acid sequence of the corresponding subunits. The specificity of one mAb, 51/24, directed against Fim2, was investigated by replacement-set analysis of a 10-residue peptide, and revealed that antibody binding to the peptide was dependent on the sequence NWPQs6 which is non-conserved in Fim3. Furthermore, proline at residue 95 was found to be essential for mAb 51/24 binding. The specific anti-Fim3 mAb, AG3A, was found to recognize the 10-residue carboxy-terminal peptide from both Fim3 and, unexpectedly, from Fim2. This result suggests that mAb AG3A serospecificity a t the protein level is determined by a conf ormational constraint which prevents mAb AG3A binding to the Fim2 C-terminal domain. Several free peptides containing amino acid residues which comprise part of the Fim2 and Fim3 epitopic domains were prepared as immunogens. One of these peptides was immunogenic in the mouse, indicating the location of a T-helper cell epitope within the peptide sequence, and induced a strong anti-peptide antibody response. The other peptides each required immunization as a conjugate with a carrier protein for anti-peptide antibody stimulation. All four anti-peptide antibody preparations only weakly recognized f imbriae-coated ELISA plates. The results of this investigation demonstrate that although short linear peptides can mimic sub-domains of non-contiguous f imbrial epitopes, they are, however, poor candidate antigens for stimulating an anti-f imbrial antibody response.

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Localisation of a receptor‐recognition domain on the S3 subunit of pertussis toxin by peptide mapping

Cited by 5 publications

References 35 publications

Aerolysin and pertussis toxin share a common receptor-binding domain

Aerolysin and pertussis toxin share a common receptor-binding domain

Spatially Addressable Combinatorial Libraries

Localization of antigenic domains on the major subunits of Bordetella pertussis serotype 2 and 3 fimbriae

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