Article
Characterization of two heparan sulphate-binding sites in the mycobacterial adhesin Hlp
Registro en:
PORTUGAL, Michelle I. et al. Characterization of two heparan sulphate-binding sites in the mycobacterial adhesin Hlp. BMC Microbiology, v.8:75, 10p, May 2008.
1471-2180
10.1186/1471-2180-8-75
Autor
Portugal, Michelle I.
Todeschini, Adriane R.
Lima, Cristiana S. de
Silva, Carlos A. M.
Borges, Ronaldo Mohana
Ottenhoff, Tom H. M.
Previato, Lucia Mendonça
Previato, Jose O.
Pessolani, Maria Cristina V.
Resumen
The histone-like Hlp protein is emerging as a key component in mycobacterial pathogenesis, being involved in the initial events of host colonization by interacting with laminin and glycosaminoglycans (GAGs). In the present study, nuclear magnetic resonance (NMR) was used to map the binding site(s) of Hlp to heparan sulfate and identify the nature of the amino acid residues directly involved in this interaction.