TY - JOUR
T1 - Interaction of human mannose-binding protein with Mycobacterium avium
AU - Polotsky, Vsevolod Y.
AU - Belisle, John T.
AU - Mikusova, Katarina
AU - Ezekowitz, R. Alan B.
AU - Joiner, Keith A.
N1 - Funding Information:
Financial support: NIH (AI-30286 to K.A.J., AI-25147 to J.T.B., and RR-02172 to R.A.B.E.); Bristol-Myers Squibb Institute (grant-in-aid to R.A.B.E.); Pediatric AIDS Foundation (grant to R.A.B.E.).
PY - 1997
Y1 - 1997
N2 - The interaction between human mannose-binding protein (MBP) and Mycobacterium avium was explored. By ELISA, calcium-dependent and mannan- inhibitable binding of human recombinant MBP (rMBP) to live M. avium was observed. Preincubation of M. avium with rMBP resulted in a 2-fold increase in uptake by human neutrophils. Mycobacterial cell wall components were assessed by ELISA for their ability to bind the carbohydrate recognition domain of rMBP. The best ligand was mannosyl-lipoarabinomannan, followed by lipomannan, phosphatidylinositol mannoside, arabinosyl-lipoarabinomannan, and dimycolated trehalose (cord factor). rMBP did not bind to partially purified lipid fractions containing glycopeptidolipids. These results are consistent with the known structural basis for rMBP ligand recognition. They suggest that MBP may play a role in host defense against M. avium by opsonizing both whole organisms and free cell wall components for internalization.
AB - The interaction between human mannose-binding protein (MBP) and Mycobacterium avium was explored. By ELISA, calcium-dependent and mannan- inhibitable binding of human recombinant MBP (rMBP) to live M. avium was observed. Preincubation of M. avium with rMBP resulted in a 2-fold increase in uptake by human neutrophils. Mycobacterial cell wall components were assessed by ELISA for their ability to bind the carbohydrate recognition domain of rMBP. The best ligand was mannosyl-lipoarabinomannan, followed by lipomannan, phosphatidylinositol mannoside, arabinosyl-lipoarabinomannan, and dimycolated trehalose (cord factor). rMBP did not bind to partially purified lipid fractions containing glycopeptidolipids. These results are consistent with the known structural basis for rMBP ligand recognition. They suggest that MBP may play a role in host defense against M. avium by opsonizing both whole organisms and free cell wall components for internalization.
UR - http://www.scopus.com/inward/record.url?scp=0030911989&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030911989&partnerID=8YFLogxK
U2 - 10.1086/520354
DO - 10.1086/520354
M3 - Article
C2 - 9129080
AN - SCOPUS:0030911989
SN - 0022-1899
VL - 175
SP - 1159
EP - 1168
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
IS - 5
ER -