Open AccessBinding of hemoglobin by Porphyromonas gingivalis
Author(s) -
Amano Atsuo,
Kuboniwa Masae,
Kataoka Kousuke,
Tazaki Katsuko,
Inoshita Eiji,
Nagata Hideki,
Tamagawa Hiroo,
Shizukuishi Satoshi
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07915.x
Subject(s) - hemin , hemoglobin , heme , porphyromonas gingivalis , biochemistry , hemeprotein , chemistry , transferrin , binding protein , plasma protein binding , population , biology , microbiology and biotechnology , bacteria , medicine , enzyme , gene , genetics , environmental health
In this study, we investigated whether Porphyromonas gingivalis can bind hemoglobin as an initial step in the acquisition of heme from hemoglobin. The binding of human hemoglobin by P. gingivalis cells was determined using [ 3 H]hemoglobin. Hemoglobin binding occurred rapidly, reversibly and specifically. A Scatchard analysis of the binding data generated a linear plot, indicating a single population of binding proteins. The apparent K d was 1.0 ± 0.19 × 10 −6 M and there were 3.2 ± 0.76 × 10 4 binding sites per cell. Hemoglobin binding was inhibited by unlabeled human hemoglobin but not by hemin and protoporphyrin IX. The binding was only partially inhibited by human serum albumin, transferrin, lactoferrin. catalase and cytochrome c. These results suggest that the ligand recognized by the binding protein may not be the heme moiety. The binding of hemoglobin considerably increased when the organisms were grown under hemin‐limited conditions. Hemoglobin bound to outer membrane proteins extracted from P. gingivalis cells on a dot blot binding assay and binding ability was lost after heating bacterial proteins. These results suggest that P. gingivalis cells interact with human hemoglobin through specific binding sites on their surfaces as a preliminary step in iron acquisition.