title: Bacterial and host-derived cationic proteins bind alpha2-laminins and enhance Mycobacterium leprae attachment to human Schwann cells.
abstract: It has recently been demonstrated that laminin alpha2 chains present on the surface of Schwann cells are involved in the process of attachment of Mycobacterium leprae to these cells. In this study, a protein in the M. leprae cell wall that was found to be capable of binding alpha2-containing laminins (merosin) was isolated and characterized. The M. leprae laminin-binding protein was identified as a 21-kDa histone-like protein (Hlp), a highly conserved cationic protein present in other species of mycobacteria. The gene that encodes this protein was PCR amplified, cloned, and expressed, and the recombinant protein was shown to bind alpha2-laminins. More significantly, when added exogenously, Hlp was able to greatly enhance the attachment of mycobacteria to ST88-14 human Schwann cells. The capacity to bind alpha2-laminins and to enhance mycobacterial adherence to Schwann cells was also found in other cationic proteins such as host-derived histones. Moreover, mutation in the hlp gene was shown not to affect the capacity of mycobacteria to bind to ST88-14 cells, suggesting that alternative adhesins and/or pathways might be used by mycobacteria during the process of adherence to Schwann cells. The potential role of Hlp as a fortuitous virulence factor contributing to the pathogenesis of M. leprae-mediated nerve damage is discussed.
authors: Laboratório de Hanseníase, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz (FIOCRUZ), Av. Brasil 4365, RJ 21045-000, Rio de Janeiro, Brazil.
authors: M A
authors: MA
authors: de Melo Marques
authors: S
authors: S
authors: Mahapatra
authors: D
authors: D
authors: Nandan
authors: T
authors: T
authors: Dick
authors: E N
authors: EN
authors: Sarno
authors: P J
authors: PJ
authors: Brennan
authors: M C
authors: MC
authors: Vidal Pessolani
mesh_terms: D018829:Adhesins, Bacterial / Q000235:genetics; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000502:physiology*; D029968:Escherichia coli Proteins; D006801:Humans; D007797:Laminin / Q000378:metabolism*; D009154:Mutation; D009166:Mycobacterium leprae / Q000235:genetics / Q000502:physiology*; D011994:Recombinant Proteins / Q000378:metabolism; D012583:Schwann Cells / Q000382:microbiology*; D017386:Sequence Homology, Amino Acid
chemical_list: D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D007797:Laminin; C121018:ML-LBP21; D011994:Recombinant Proteins; C116822:hns protein, E coli; C102645:laminin alpha 2