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PMID: 9784525 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Neisseria gonorrhoeae heme biosynthetic mutants utilize heme and hemoglobin as a heme source but fail to grow within epithelial cells.

Infection and immunity ·Vol. 66 ·No. 11 ·1998-11-00 ·Pages 5215-23

Turner PC, Thomas CE, Elkins C, Clary S, Sparling PF

Abstract

Many bacterial pathogens, including pathogenic neisseriae, can use heme as an iron source for growth. To study heme utilization by Neisseria gonorrhoeae, two heme biosynthetic mutants were constructed, one with a mutation in hemH (the gene encoding ferrochelatase) and one with a mutation in hemA (the gene encoding gamma-glutamyl tRNA reductase). The hemH mutant failed to grow without an exogenous supply of heme or hemoglobin, whereas the hemA mutant failed to grow unless heme, hemoglobin, or heme precursors were present. Growth of the mutants with hemoglobin required expression of the hemoglobin receptor (HpuAB) and was TonB dependent. However, growth with heme required neither HpuAB nor TonB. An fbpA mutant grew normally when either heme or hemoglobin was present in the medium. The heme biosynthetic mutants showed reduced intracellular survival, compared to the parent strain, within A-431 endocervical epithelial cell cultures. These studies demonstrate that in addition to synthesizing their own heme, N. gonorrhoeae strains are able to internalize and utilize exogenous heme independently of FbpA but appear unable to obtain heme from within epithelial cells for growth.

MeSH Terms
Aldehyde Oxidoreductases/genetics Bacterial Outer Membrane Proteins Bacterial Proteins/genetics Carrier Proteins/genetics Cell Line Cervix Uteri Epithelial Cells/metabolism,microbiology Female Heme/biosynthesis,metabolism,physiology Hemoglobins/metabolism Humans Intracellular Fluid/microbiology,physiology Iron/metabolism Iron-Binding Proteins Mutagenesis, Site-Directed Neisseria gonorrhoeae/genetics,growth & development,metabolism Periplasmic Binding Proteins Phenotype
Chemicals
Bacterial Outer Membrane Proteins Bacterial Proteins Carrier Proteins Hemoglobins Iron-Binding Proteins Periplasmic Binding Proteins Heme Iron Aldehyde Oxidoreductases glutamyl tRNA reductase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Turner P C
Department of Medicine, School of Medicine, University of North Carolina, Chapel Hill, North Carolina 27599, USA. pturner@med.unc.edu
Thomas C E
Elkins C
Clary S
Sparling P F
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
1998-11-00
Pages
5215-23
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC108651
Subset
IM
Grants
NIAID NIH HHS · R37 AI026837 · United States
NIAID NIH HHS · R01 AI032493 · United States
NIAID NIH HHS · AI 32493 · United States
NIAID NIH HHS · U19 AI031496 · United States
NIAID NIH HHS · R01 AI026837 · United States
NIAID NIH HHS · AI 31496 · United States
NIAID NIH HHS · AI 26837 · United States
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