TY - JOUR
T1 - Role of N-acetylglucosamine within core lipopolysaccharide of several species of Gram-negative bacteria in targeting the DC-SIGN (CD209)
AU - Zhang, Pei
AU - Snyder, Scott
AU - Feng, Peter
AU - Azadi, Parastoo
AU - Zhang, Shusheng
AU - Bulgheresi, Silvia
AU - Sanderson, Kenneth E.
AU - He, Johnny
AU - Klena, John
AU - Chen, Tie
PY - 2006/9/15
Y1 - 2006/9/15
N2 - Our recent studies have shown that the dendritic cell-specific ICAM nonintegrin CD209 (DC-SIGN) specifically binds to the core LPS of Escherichia coli K12 (E. coli), promoting bacterial adherence and phagocytosis. In this current study, we attempted to map the sites within the core LPS that are directly involved in LPS-DC-SIGN interaction. We took advantage of four sets of well-defined core LPS mutants, which are derived from E. coli, Salmonella enterica serovar Typhimurium, Neisseria gonorrhoeae, and Haemophilus ducreyi and determined interaction of each of these four sets with DC-SIGN. Our results demonstrated that N-acetylglucosamine (GlcNAc) sugar residues within tine core LPS in these bacteria play an essential role in targeting the DC-SIGN receptor. Our results also imply that DC-SIGN is an innate immune receptor and the interaction of bacterial core LPS and DC-SIGN may represent a primeval interaction between Gram-negative bacteria and host phagocytic cells.
AB - Our recent studies have shown that the dendritic cell-specific ICAM nonintegrin CD209 (DC-SIGN) specifically binds to the core LPS of Escherichia coli K12 (E. coli), promoting bacterial adherence and phagocytosis. In this current study, we attempted to map the sites within the core LPS that are directly involved in LPS-DC-SIGN interaction. We took advantage of four sets of well-defined core LPS mutants, which are derived from E. coli, Salmonella enterica serovar Typhimurium, Neisseria gonorrhoeae, and Haemophilus ducreyi and determined interaction of each of these four sets with DC-SIGN. Our results demonstrated that N-acetylglucosamine (GlcNAc) sugar residues within tine core LPS in these bacteria play an essential role in targeting the DC-SIGN receptor. Our results also imply that DC-SIGN is an innate immune receptor and the interaction of bacterial core LPS and DC-SIGN may represent a primeval interaction between Gram-negative bacteria and host phagocytic cells.
UR - http://www.scopus.com/inward/record.url?scp=33748502748&partnerID=8YFLogxK
U2 - 10.4049/jimmunol.177.6.4002
DO - 10.4049/jimmunol.177.6.4002
M3 - Article
C2 - 16951363
AN - SCOPUS:33748502748
SN - 0022-1767
VL - 177
SP - 4002
EP - 4011
JO - Journal of Immunology
JF - Journal of Immunology
IS - 6
ER -