Capture of heat-killed Mycobacterium bovis bacillus Calmette-Guérin by intelectin-1deposited on cell surfaces
Loading...
Date
2009-05
Access
Authors
Tsuji, Shoutaro
Yamashita, Makiko
Hoffman, Donald R.
Nishiyama, Akihito
Shinohara, Tsutomu
Ohtsu, Takashi
Shibata, Yoshimi
Journal Title
Journal ISSN
Volume Title
Publisher
East Carolina University
Abstract
Intelectin is an extracellular animal lectin found in chordata. Although human and mouse intelectin-1 recognize galactofuranosyl residues included in cell walls of various microorganisms, the physiological function of mammalian intelectin had been unclear. In this study, we found that human intelectin-1 was a serum protein and bound to Mycobacterium bovis bacillus Calmette-Gu´erin (BCG). Human intelectin-1-binding to BCG was inhibited by Ca2+- depletion, galactofuranosyl disaccharide, ribose, or xylose, and was dependent on the trimeric structure of human intelectin-1. Although monomeric, mouse intelectin-1 bound to BCG, with its C-terminal region contributing to efficient binding. Human intelectin-1-transfected cells not
only secreted intelectin-1 into culture supernatant but also expressed intelectin-1 on the cell surface. The cell surface intelectin-1 was not a glycosylphosphatidylinositolanchored membrane protein. Intelectin-1-transfected cells captured BCG more than untransfected cells, and the BCG adherence was inhibited by an inhibitory saccharide of intelectin-1. Intelectin-1-preincubated cells took up BCG more than untreated cells, but the adhesion of intelectin-1- bound BCG was the same as that of untreated BCG. Mouse macrophages phagocytosedBCGmore efficiently in medium containing mouse intelectin-1 than in control medium. These results indicate that intelectin is a host defense lectin that assists phagocytic clearance of microorganisms. Originally published Glycobiology, Vol. 19, No. 5, May 2009
Description
Keywords
Citation
Glycobiology; 19:5 p. 518-526
DOI
10.1093/glycob/cwp013