Related Experiment Video
Updated: Jun 29, 2026

Porphyromonas gingivalis as a Model Organism for Assessing Interaction of Anaerobic Bacteria with Host Cells
Published on: December 17, 2015
Human alpha- and beta-defensins bind to immobilized adhesins from Porphyromonas gingivalis
Deborah E Dietrich1, Xiangjun Xiao, Deborah V Dawson
1Dows Institute for Dental Research, College of Dentistry, The University of Iowa, Iowa City, Iowa 52242, USA.
Abstract:
Human neutrophil peptide alpha-defensins (HNPs) and human beta-defensins (HBDs) are small well-characterized peptides with broad antimicrobial activities and a diversity of innate immune functions. Although the interactions of defensins with bacteria and their membranes have been well characterized, the interactions of defensins with bacterial adhesins have not. Here we determine if HNPs and HBDs bind to the immobilized adhesins of Porphyromonas gingivalis strain 381, recombinant hemagglutinin B (rHagB) and recombinant fimbrillin A (rFimA), by surface plasmon resonance spectroscopy. Association of HNPs and HBDs with rHagB or rFimA was dose dependent and defensin specific. HBD3, HNP-2, and HNP-1 bound more readily to immobilized rHagB than HBD2 and HBD1 did. HNP-2, HNP-1, and HBD3 bound more readily to immobilized rFimA than HBD1 and HBD2 did. Binding of defensins to adhesins may serve to prevent microbial adherence to tissues, attenuate proinflammatory cytokine responses, and facilitate delivery of bound antigen to antigen-presenting cells with defensin receptors.
Related Concept Videos
Adherens Junctions
Adherens Junctions are Dynamic
The endothelial cells...
Fimbriae, Pili, and Axial Filaments
The Oral Microbiota
Antimicrobial Proteins
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
Determinants of Bacterial Pathogenicity and Virulence
Biofilms

