TY - JOUR
T1 - Biochemical analysis of lactoferrin receptors in the Neisseriaceae
T2 - Identification of a second bacterial lactoferrin receptor protein
AU - Bonnah, Robert A.
AU - Yu, Rong Hua
AU - Schryvers, Anthony B.
N1 - Funding Information:
This workwas supported in part by the Medical Research Council of Canada Grant number MT10350, and also from Connaught Research Laboratories, Willowdale, Ontario. Thanks
PY - 1995
Y1 - 1995
N2 - Bacterial transferrin receptors that have been described in the families Pasteurellaceae and Neisseriaceae are composed of two receptor proteins, transferrin binding proteins 1 and 2 (Tbp1 and Tbp2). In contrast, bacterial lactoferrin receptors have only been described for human pathogens in the family Neisseriaceae, and were believed to consist of a single protein, Lbp1, which is highly homologous to Tbp1. We describe a modified affinity isolation procedure that facilities isolation of a second lactoferrin receptor protein Lbp2 (a presumptive Tbp2 homologue) from Neisseria meningitidis, Moraxella catarrhalis and Moraxella bovis using immobilized lactoferrin. Antiserum specific for either the M. catarrhalis Tbp1+2 molecules, the M. catarrhalis Lbp1 molecule, or for a commercial preparation of human lactoferrin did not react on western blots with the same organisms’ affinity purified Lbp2. In addition, the M. catarrhalis Lbp2 could be isolated in a functional form without contaminating Lbp1 or Tbp1+2. We also demonstrate that the bovine pathogen, M. bovis, produces functional transferrin and lactoferrin receptors specific for the bovine forms of these glycoproteins. A putative IbpB gene, recently speculated to reside immediately upstream of the N. meningitidis Lbp1 structural gene, IbpA, likely encodes the newly isolated Lbp2 protein from this bacterial species.
AB - Bacterial transferrin receptors that have been described in the families Pasteurellaceae and Neisseriaceae are composed of two receptor proteins, transferrin binding proteins 1 and 2 (Tbp1 and Tbp2). In contrast, bacterial lactoferrin receptors have only been described for human pathogens in the family Neisseriaceae, and were believed to consist of a single protein, Lbp1, which is highly homologous to Tbp1. We describe a modified affinity isolation procedure that facilities isolation of a second lactoferrin receptor protein Lbp2 (a presumptive Tbp2 homologue) from Neisseria meningitidis, Moraxella catarrhalis and Moraxella bovis using immobilized lactoferrin. Antiserum specific for either the M. catarrhalis Tbp1+2 molecules, the M. catarrhalis Lbp1 molecule, or for a commercial preparation of human lactoferrin did not react on western blots with the same organisms’ affinity purified Lbp2. In addition, the M. catarrhalis Lbp2 could be isolated in a functional form without contaminating Lbp1 or Tbp1+2. We also demonstrate that the bovine pathogen, M. bovis, produces functional transferrin and lactoferrin receptors specific for the bovine forms of these glycoproteins. A putative IbpB gene, recently speculated to reside immediately upstream of the N. meningitidis Lbp1 structural gene, IbpA, likely encodes the newly isolated Lbp2 protein from this bacterial species.
KW - Iron acquisition
KW - Lactoferrin
KW - Moraxella
KW - Neisseria
KW - Receptor
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U2 - 10.1016/S0882-4010(96)80002-7
DO - 10.1016/S0882-4010(96)80002-7
M3 - Article
C2 - 8778564
AN - SCOPUS:0029587287
SN - 0882-4010
VL - 19
SP - 285
EP - 297
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
IS - 5
ER -