Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily.

Floris J Bikker, Antoon J M Ligtenberg, Kamran Nazmi, Enno C I Veerman, Wim van't Hof, Jan G M Bolscher, Annemarie Poustka, Arie V Nieuw Amerongen, Jan Mollenhauer

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Salivary agglutinin is encoded by DMBT1 and identical to gp-340, a member of the scavenger receptor cysteine-rich (SRCR) superfamily. Salivary agglutinin/DMBT1 is known for its Streptococcus mutans agglutinating properties. This 300-400 kDa glycoprotein is composed of conserved peptide motifs: 14 SRCR domains that are separated by SRCR-interspersed domains (SIDs), 2 CUB (C1r/C1s Uegf Bmp1) domains, and a zona pellucida domain. We have searched for the peptide domains of agglutinin/DMBT1 responsible for bacteria binding. Digestion with endoproteinase Lys-C resulted in a protein fragment containing exclusively SRCR and SID domains that binds to S. mutans. To define more closely the S. mutans-binding domain, consensus-based peptides of the SRCR domains and SIDs were designed and synthesized. Only one of the SRCR peptides, designated SRCRP2, and none of the SID peptides bound to S. mutans. Strikingly, this peptide was also able to induce agglutination of S. mutans and a number of other bacteria. The repeated presence of this peptide in the native molecule endows agglutinin/DMBT1 with a general bacterial binding feature with a multivalent character. Moreover, our studies demonstrate for the first time that the polymorphic SRCR domains of salivary agglutinin/DMBT1 mediate ligand interactions.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume277
Issue number35
Pages (from-to)32109-15
Number of pages6
ISSN0021-9258
DOIs
Publication statusPublished - 30. Aug 2002

Fingerprint

Scavenger Receptors
Agglutinins
Cysteine
Bacteria
Peptides
Zona Pellucida
Peptide Receptors
glycoprotein 340
Glycoproteins
Ligands
Molecules

Keywords

  • Agglutination
  • Agglutinins
  • Amino Acid Sequence
  • Binding Sites
  • Consensus Sequence
  • Cysteine
  • Humans
  • Lysine
  • Models, Molecular
  • Molecular Sequence Data
  • Parotid Gland
  • Peptide Fragments
  • Polymorphism, Genetic
  • Protein Conformation
  • Receptors, Cell Surface
  • Saliva
  • Salivary Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Streptococcus mutans

Cite this

Bikker, F. J., Ligtenberg, A. J. M., Nazmi, K., Veerman, E. C. I., van't Hof, W., Bolscher, J. G. M., ... Mollenhauer, J. (2002). Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily. Journal of Biological Chemistry, 277(35), 32109-15. https://doi.org/10.1074/jbc.M203788200
Bikker, Floris J ; Ligtenberg, Antoon J M ; Nazmi, Kamran ; Veerman, Enno C I ; van't Hof, Wim ; Bolscher, Jan G M ; Poustka, Annemarie ; Nieuw Amerongen, Arie V ; Mollenhauer, Jan. / Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 35. pp. 32109-15.
@article{bb3ce360596d11ddb1a1000ea68e967b,
title = "Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily.",
abstract = "Salivary agglutinin is encoded by DMBT1 and identical to gp-340, a member of the scavenger receptor cysteine-rich (SRCR) superfamily. Salivary agglutinin/DMBT1 is known for its Streptococcus mutans agglutinating properties. This 300-400 kDa glycoprotein is composed of conserved peptide motifs: 14 SRCR domains that are separated by SRCR-interspersed domains (SIDs), 2 CUB (C1r/C1s Uegf Bmp1) domains, and a zona pellucida domain. We have searched for the peptide domains of agglutinin/DMBT1 responsible for bacteria binding. Digestion with endoproteinase Lys-C resulted in a protein fragment containing exclusively SRCR and SID domains that binds to S. mutans. To define more closely the S. mutans-binding domain, consensus-based peptides of the SRCR domains and SIDs were designed and synthesized. Only one of the SRCR peptides, designated SRCRP2, and none of the SID peptides bound to S. mutans. Strikingly, this peptide was also able to induce agglutination of S. mutans and a number of other bacteria. The repeated presence of this peptide in the native molecule endows agglutinin/DMBT1 with a general bacterial binding feature with a multivalent character. Moreover, our studies demonstrate for the first time that the polymorphic SRCR domains of salivary agglutinin/DMBT1 mediate ligand interactions.",
keywords = "Agglutination, Agglutinins, Amino Acid Sequence, Binding Sites, Consensus Sequence, Cysteine, Humans, Lysine, Models, Molecular, Molecular Sequence Data, Parotid Gland, Peptide Fragments, Polymorphism, Genetic, Protein Conformation, Receptors, Cell Surface, Saliva, Salivary Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Streptococcus mutans",
author = "Bikker, {Floris J} and Ligtenberg, {Antoon J M} and Kamran Nazmi and Veerman, {Enno C I} and {van't Hof}, Wim and Bolscher, {Jan G M} and Annemarie Poustka and {Nieuw Amerongen}, {Arie V} and Jan Mollenhauer",
year = "2002",
month = "8",
day = "30",
doi = "10.1074/jbc.M203788200",
language = "English",
volume = "277",
pages = "32109--15",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "35",

}

Bikker, FJ, Ligtenberg, AJM, Nazmi, K, Veerman, ECI, van't Hof, W, Bolscher, JGM, Poustka, A, Nieuw Amerongen, AV & Mollenhauer, J 2002, 'Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily.', Journal of Biological Chemistry, vol. 277, no. 35, pp. 32109-15. https://doi.org/10.1074/jbc.M203788200

Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily. / Bikker, Floris J; Ligtenberg, Antoon J M; Nazmi, Kamran; Veerman, Enno C I; van't Hof, Wim; Bolscher, Jan G M; Poustka, Annemarie; Nieuw Amerongen, Arie V; Mollenhauer, Jan.

In: Journal of Biological Chemistry, Vol. 277, No. 35, 30.08.2002, p. 32109-15.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily.

AU - Bikker, Floris J

AU - Ligtenberg, Antoon J M

AU - Nazmi, Kamran

AU - Veerman, Enno C I

AU - van't Hof, Wim

AU - Bolscher, Jan G M

AU - Poustka, Annemarie

AU - Nieuw Amerongen, Arie V

AU - Mollenhauer, Jan

PY - 2002/8/30

Y1 - 2002/8/30

N2 - Salivary agglutinin is encoded by DMBT1 and identical to gp-340, a member of the scavenger receptor cysteine-rich (SRCR) superfamily. Salivary agglutinin/DMBT1 is known for its Streptococcus mutans agglutinating properties. This 300-400 kDa glycoprotein is composed of conserved peptide motifs: 14 SRCR domains that are separated by SRCR-interspersed domains (SIDs), 2 CUB (C1r/C1s Uegf Bmp1) domains, and a zona pellucida domain. We have searched for the peptide domains of agglutinin/DMBT1 responsible for bacteria binding. Digestion with endoproteinase Lys-C resulted in a protein fragment containing exclusively SRCR and SID domains that binds to S. mutans. To define more closely the S. mutans-binding domain, consensus-based peptides of the SRCR domains and SIDs were designed and synthesized. Only one of the SRCR peptides, designated SRCRP2, and none of the SID peptides bound to S. mutans. Strikingly, this peptide was also able to induce agglutination of S. mutans and a number of other bacteria. The repeated presence of this peptide in the native molecule endows agglutinin/DMBT1 with a general bacterial binding feature with a multivalent character. Moreover, our studies demonstrate for the first time that the polymorphic SRCR domains of salivary agglutinin/DMBT1 mediate ligand interactions.

AB - Salivary agglutinin is encoded by DMBT1 and identical to gp-340, a member of the scavenger receptor cysteine-rich (SRCR) superfamily. Salivary agglutinin/DMBT1 is known for its Streptococcus mutans agglutinating properties. This 300-400 kDa glycoprotein is composed of conserved peptide motifs: 14 SRCR domains that are separated by SRCR-interspersed domains (SIDs), 2 CUB (C1r/C1s Uegf Bmp1) domains, and a zona pellucida domain. We have searched for the peptide domains of agglutinin/DMBT1 responsible for bacteria binding. Digestion with endoproteinase Lys-C resulted in a protein fragment containing exclusively SRCR and SID domains that binds to S. mutans. To define more closely the S. mutans-binding domain, consensus-based peptides of the SRCR domains and SIDs were designed and synthesized. Only one of the SRCR peptides, designated SRCRP2, and none of the SID peptides bound to S. mutans. Strikingly, this peptide was also able to induce agglutination of S. mutans and a number of other bacteria. The repeated presence of this peptide in the native molecule endows agglutinin/DMBT1 with a general bacterial binding feature with a multivalent character. Moreover, our studies demonstrate for the first time that the polymorphic SRCR domains of salivary agglutinin/DMBT1 mediate ligand interactions.

KW - Agglutination

KW - Agglutinins

KW - Amino Acid Sequence

KW - Binding Sites

KW - Consensus Sequence

KW - Cysteine

KW - Humans

KW - Lysine

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Parotid Gland

KW - Peptide Fragments

KW - Polymorphism, Genetic

KW - Protein Conformation

KW - Receptors, Cell Surface

KW - Saliva

KW - Salivary Proteins

KW - Sequence Alignment

KW - Sequence Homology, Amino Acid

KW - Streptococcus mutans

U2 - 10.1074/jbc.M203788200

DO - 10.1074/jbc.M203788200

M3 - Journal article

C2 - 12050164

VL - 277

SP - 32109

EP - 32115

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 35

ER -