Bacterial and host-derived cationic proteins bind α2-laminins and enhance Mycobacterium leprae attachment to human Schwann cells

Maria Angela De Melo Marques, Sebabrata Mahapatra, Devki Nandan, Thomas Dick, Euzenir Nunes Sarno, Patrick Joseph Brennan, Maria Cristina Vidal Pessolani

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It has recently been demonstrated that laminin α2 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 α2-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 α2-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 α2-laminins and to enhance mycobacterial adherence to Schwann cells was also found in other cationic proteins such as host-derived histories. 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. (C) 2000 Editions scientifiques et medicales Elsevier SAS.

Original languageEnglish (US)
Pages (from-to)1407-1417
Number of pages11
JournalMicrobes and Infection
Issue number12
StatePublished - Jan 1 2000


All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Infectious Diseases


  • Adherence
  • Histone-like protein
  • Laminin-binding protein
  • Mycobacterium leprae
  • Schwann cell

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