Characterization of the Fibronectin Binding Motif for a Unique Mycobacterial Fibronectin Attachment Protein, FAP

Abstract

The attachment of mycobacteria to fibronectin is well documented (1, 2). All tested species including Mycobacterium bovis strain BCG, Mycobacterium tuberculosis, Mycobacterium kansasii, Mycobacterium avium, Mycobacterium leprae, and Mycobacterium smegmatis were observed to attach to fibronectin (3-5). In studies on M. bovis BCG-mediated immunotherapy, which is the treatment of choice for superficial bladder cancer, fibronectin attachment was shown to be necessary for the expression of antitumor activity (2). In addition, the attachment and internalization of M. bovis BCG, M. avium, and M. leprae by epithelial cells and Schwann cells also were shown to be dependent on bacterial attachment to fibronectin (4, 6, 7). Thus, an understanding of the interaction between mycobacterial proteins mediating attachment to fibronectin is needed.Two distinct mycobacterial proteins or protein complexes, fibronectin attachment protein (FAP) 1 and proteins of the antigen 85 complex, have been linked to mycobacterial attachment to fibronectin (8, 9). The interaction of proteins from the antigen 85 complex with fibronectin has been characterized using recombinant 85A, 85B, and 85C proteins (10 -12). The best characterized of the complex is the 85B protein. In the present study, the amino acids required for fibronectin binding of the FAP-A-(269 -292) peptide were determined us-

Novel Mycobacteria Antigen 85 Complex Binding Motif on Fibronectin

“…These results indicate that the Ag85-Fn interaction accounts for only a portion of the ability of a MAP cell to adhere to a host cell. Other surface antigens such as FbpD, ModD, or unidentified proteins of MAP K-10 probably participate in additional ECM interactions (44,45,(53)(54)(55).…”

Mycobacterium aviumsubsp.paratuberculosisFibronectin Attachment Protein Facilitates M-Cell Targeting and Invasion through a Fibronectin Bridge with Host Integrins

“…The discrete Peyer's patches in the intestinal tracts of other mammals and the jejunum of ruminants are secondary lymphoid organs, in which an adaptive immune response can be initiated following exposure to foreign antigens. In contrast, the continuous Peyer's patch in the ruminant ileum is a primary lymphoid organ, wherein B-cell development occurs (36).Fibronectin attachment proteins (FAPs) are a family of fibronectin (FN)-binding proteins present in several species of mycobacteria (25,(28)(29)(30)42). Attachment and internalization of Mycobacterium bovis BCG, M. leprae, and M. avium subsp.…”

Cellular attachment and internalization of cationic liposomes containing mycobacterial cell wall

“…Since the cellular association and internalization of BCG components are necessary events for the activation of immunity to BCG and for the induction of antitumour effect 5,11 . Through this present work, we have demonstrated the cellular attachment and uptake of BCG cell wall in murine bladder tumour cells by using cationic liposomes as a novel BCG cell wall delivery system.…”

“…After instillation of the live BCG into the bladder, the bacteria is thought to bind to the urothelial lining. This binding is dependent on the interaction of a fibronectin attachment protein (FAP) on the surface of BCG with fibronectin, a matrix protein, presenting onto the surface of bladder epithelial cells 5 . Subsequently, BCG is taken up by bladder epithelial cells and BCG-derived antigens are then processed and presented on cell surface for immune recognition.…”