The respiratory pathogen moraxella catarrhalis binds to laminin via ubiquitous surface proteins A1 and A2.
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.
Tan
Thuan Tong
TT
Medical Microbiology, Department of Laboratory Medicine, Malmo University Hospital, Lund University, SE-205 02 Malmo, Sweden.
Forsgren
Arne
A
Riesbeck
Kristian
K
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
D001425:Bacterial Outer Membrane Proteins; D007797:Laminin; C089675:UspA protein, Moraxella catarrhalis