The calcium-induced conformation and glycosylation of scavenger-rich cysteine repeat (SRCR) domains of glycoprotein 340 influence the high affinity interaction with antigen I/II homologs

Academic Article

Abstract

  • Background: AgI/II homolog interaction with GP340 is crucial for bacterial attachment to tooth surface. Results: Tandem SRCR domains efficiently adhere/aggregate bacteria. Calcium-induced conformational switch and O-linked carbohydrates of SRCRs are necessary for the interaction with AgI/II homologs. Conclusion: High affinity interactions are dictated by calcium and carbohydrates. Significance: Oral streptococci adhere to specific calcium-induced conformation of immobilized SRCRs and to its carbohydrates. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
  • Digital Object Identifier (doi)

    Author List

  • Purushotham S; Deivanayagam C
  • Start Page

  • 21877
  • End Page

  • 21887
  • Volume

  • 289
  • Issue

  • 32