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Characterization of two heparan sulphate-binding sites in the mycobacterial adhesin Hlp |
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| Authors: | Michelle I Portugal Adriane R Todeschini Cristiana S de Lima Carlos AM Silva Ronaldo Mohana-Borges Tom HM Ottenhoff Lucia Mendonça-Previato Jose O Previato Maria CV Pessolani |
| Affiliation: | (1) Laboratrio de Microbiologia Celular,, Instituto Oswaldo Cruz,FIOCRUZ, Av. Brasil 4365 Manguinhos, Rio de Janeiro, RJ, 21045-900, Brazil;(2) Laboratrio de Glicobiologia, Instituto de BiofEsica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Tropowsky, Rio de Janeiro, RJ, 21949-900, Brazil;(3) Laboratrio de Genomica Estrutural, Instituto de Biofsica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Tropowsky, Rio de Janeiro, RJ, 21949-900, Brazil;(4) Department of Immunohematology and Blood Transfusion, Leiden University Medical Center, Building 1 E3-Q, Leiden, RC, P.O. box 9600, 2300, The Netherlands |
| Abstract: | BackgroundThe 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. |
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