title: The respiratory pathogen moraxella catarrhalis binds to laminin via ubiquitous surface proteins A1 and A2.
abstract: Moraxella catarrhalis is one of the leading causes of exacerbations in chronic obstructive pulmonary disease (COPD). In the present article, we show that moraxella (n=15) binds to the major basement-membrane glycoprotein laminin, which is thickened in the airways of smokers. Using clinical strains of M. catarrhalis and their corresponding ubiquitous surface protein (Usp) A1/A2 mutants, we demonstrate that UspA1 and UspA2 are important for the laminin interaction. Binding assays with recombinant proteins demonstrated that the binding regions are localized within the N-terminal fragments, where both proteins form a globular head. Thus, UspA1/A2-dependent interactions with laminin might promote bacterial adhesion, particularly in smokers with COPD.
authors.affiliation: Medical Microbiology, Department of Laboratory Medicine, Malmo University Hospital, Lund University, SE-205 02 Malmo, Sweden.
authors.forename: Thuan Tong
authors.initials: TT
authors.lastname: Tan
authors.forename: Arne
authors.initials: A
authors.lastname: Forsgren
authors.forename: Kristian
authors.initials: K
authors.lastname: Riesbeck
mesh_terms: D001422:Bacterial Adhesion / Q000502:physiology; D001425:Bacterial Outer Membrane Proteins / Q000502:physiology*; D006801:Humans; D007797:Laminin / Q000502:physiology*; D001936:Moraxella catarrhalis / Q000472:pathogenicity / Q000502:physiology*; D045828:Moraxellaceae Infections / Q000150:complications* / Q000382:microbiology; D029424:Pulmonary Disease, Chronic Obstructive / Q000150:complications* / Q000382:microbiology; D012907:Smoking / Q000009:adverse effects
chemical_list: D001425:Bacterial Outer Membrane Proteins; D007797:Laminin; C089675:UspA protein, Moraxella catarrhalis