title: Interaction with Borrelia burgdorferi causes increased expression of the CR3 integrin and increased binding affinity to fibronectin via CR3.
abstract: We have previously demonstrated that the alphaMbeta2 integrin (known as CR3 or Mac-1) expressed on neutrophils (PMNs) and/or on CHO Mac-1 transfected cells,in the presence of serum complement binds B. burgdorferi and promotes an increased non -opsonic adhesion, in the presence of serum complement. In this study we demonstrate that: 1) living motile B. burgdorferiand recombinant lipidated OspA and OspC, up-regulate CR3 expression on PMNs; 2) in the absence of serum, B. burgdorferi induces increased adhesion of CHO cells expressing CR3 to fibronectin, an extracellular matrix protein. Both the I-domain and the lectin-like domain of CR3 are involved in the binding recognition and activation because mAb anti I-domain and N-acetyl-glucosamine inhibit cell adhesion to fibronectin. These data indicate that B. burgdorferi whole cells, but not Osps, activate CR3 integrin; since this receptor plays a key role in priming neutrophils to important inflammatory events, the interaction of B. burgdorferi with neutrophils via the CR3 may enhance their role both in defence and in disease.
authors.affiliation: Dipartimento di Scienze Biomediche, Università di Trieste, Italy. Cinco@FC.UNIV.Trieste.it
authors.forename: M
authors.initials: M
authors.lastname: Cinco
authors.forename: E
authors.initials: E
authors.lastname: Panfili
authors.forename: G
authors.initials: G
authors.lastname: Presani
authors.forename: S
authors.initials: S
authors.lastname: Perticarari
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000494:pharmacology; D000942:Antigens, Bacterial; D000954:Antigens, Surface / Q000378:metabolism; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001428:Bacterial Vaccines; D001665:Binding Sites; D015748:Borrelia burgdorferi Group / Q000502:physiology*; D016466:CHO Cells; D002448:Cell Adhesion / Q000502:physiology; D006224:Cricetinae; D005353:Fibronectins / Q000502:physiology*; D005786:Gene Expression Regulation; D006801:Humans; D066298:In Vitro Techniques; D008074:Lipoproteins / Q000378:metabolism; D022123:Lyme Disease Vaccines / Q000378:metabolism; D016177:Macrophage-1 Antigen / Q000235:genetics* / Q000502:physiology; D009504:Neutrophils / Q000382:microbiology* / Q000502:physiology*; D011994:Recombinant Proteins / Q000378:metabolism; D014162:Transfection; D015854:Up-Regulation
chemical_list: D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D005353:Fibronectins; D008074:Lipoproteins; D022123:Lyme Disease Vaccines; D016177:Macrophage-1 Antigen; C072045:OspA protein; C079616:OspC protein; D011994:Recombinant Proteins