Open AccessThe 70 kilodalton iron regulated protein of Neisseria meningitidis is not the human transferrin receptor
Author(s) -
Ala'Aldeen D.A.,
Davies Heather A.,
Wall R.A.,
Borriello S.P.
Publication year - 1990
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.1574-6968.1990.tb04171.x
Subject(s) - transferrin , bacterial outer membrane , neisseria meningitidis , transferrin receptor , chemistry , western blot , microbiology and biotechnology , biochemistry , biology , bacteria , gene , escherichia coli , genetics
Neisseria meningitidis is able to chelate iron from human transferrin (HTF), the main sequestrator of extracellular iron in vivo. Previous workers have reported that a ca. 70 kilodalton (kDa) iron regulated outer membrane protein (FeRP‐70) is a highly specific receptor for HTF. We have examined the interaction between the iron regulated outer membrane proteins (OMP's) and HTF, using HTF and rabbit anti HTF, as well as gold labelled HTF (Au‐HTF) to blot OMP's of various serogroups and serotypes of N. meningitidis . Also, we used monospecific rabbit anti FeRP‐70 in competitive experiments to determine the role of FeRP‐70 in HTF‐binding. Single proteins (molecular weights range ca. 60 to ca. 90 kDa) were identified in the OMP's from each strain which reacted with HTF. HTF failed to block the reaction between FeRP‐70 and the OMP's, conversely anti FeRP‐70 failed to block the HTF‐binding reaction. We believe that the 70 kDa iron regulated protein of N. meningitidis is not a human transferrin receptor.