Molecular Characterization of theEscherichia coliFimH Adhesin

Molecular characterization of the mycobacterial heparin-binding hemagglutinin, a mycobacterial adhesin.

Although it generally is accepted that the interaction of Mycobacterium tuberculosis with alveolar macrophages is a key step in the pathogenesis of tuberculosis, interactions with other cell types, especially epithelial cells, also may be important. In this study we describe the molecular characterization of a mycobacterial heparin-binding hemagglutinin (HBHA), a protein that functions as an ad...

Streptococcus sanguis expresses a 150-kilodalton two-domain adhesin: characterization of several independent adhesin epitopes.

Streptococcus sanguis binds to saliva-coated hydroxylapatite (sHA), an in vitro model of the enamel pellicle. To learn if more than one adhesin functions during adhesion, 12 reactive monoclonal antibodies (MAbs) were isolated by screening against both adhesive and nonadhesive strains. Two of these MAbs, 1.1 and 1.2, inhibited adhesion in a dose-dependent fashion, although maximum inhibition wit...

Molecular Characterization of Aureobasidium Species in Iran

Background: Members of this genus Aureobasidium are ubiquitous microorganisms which can be isolated from wide ranges of substrates such as plant materials (phyllosphere, plant debris, bark, roots, fruits and wood), soil, dead wood, air, and as rare etiologic agent of pheohyphomycosis, keratomycosis, septicemia, peritoneal sepsis, and dermatological infections in human. Very little is known on t...

Structure refinement of the OpcA adhesin using molecular dynamics.

OpcA from Neisseria meningitidis, the causative agent of meningococcal meningitis and septicemia, is an integral outer membrane protein that facilitates meningococcal adhesion through binding the proteoglycan receptors of susceptible cells. Two structures of OpcA have been determined by x-ray diffraction to 2 A resolution, revealing dramatically different conformations in the extracellular loop...

Characterization of the interaction between the chlamydial adhesin OmcB