Expression of the CopB outer membrane protein by Moraxella catarrhalis is regulated by iron and affects iron acquisition from transferrin and lactoferrin

Christoph Aebi, Barbara Stone, Margaret Beucher, Leslie D. Cope, Isobel Maciver, Sharon E. Thomas, George H. Mccracken, P. Frederick Sparling, Eric J. Hansen

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

The amino acid sequence of the cell-surface-exposed, 81-kDa CopB outer membrane protein of Moraxella catarrhalis was found to be similar to those of TonB-dependent outer membrane proteins of other gram-negative bacteria. Expression of CopB was affected by the availability of iron in the growth medium, and the extent of overexpression of CopB in response to iron limitation varied widely among the M. catarrhalis strains tested. Wild-type M. catarrhalis strains were found to be able to utilize ferric citrate, transferrin, lactoferrin, and heme as sources of iron for growth in vitro. However, an isogenic copB mutant was severely impaired in its ability to utilize transferrin and lactoferrin as sole sources of iron for growth, whereas this same mutant grew similarly to the wild-type parent strain when supplied with ferric citrate as the iron source. The copB mutant was not significantly different from its wild-type parent strain in its ability to bind transferrin and lactoferrin. In addition, the wild-type parent strain and the copB mutant exhibited equivalent rates of uptake of 55Fe from ferric citrate. However, the copB mutant was markedly less able than the wild-type strain to take up 55Fe from transferrin and lactoferrin. These results indicate that lack of expression of the CopB protein exerts a direct or indirect effect on the ability of M. catarrhalis to utilize iron bound to certain carrier proteins.

Original languageEnglish (US)
Pages (from-to)2024-2030
Number of pages7
JournalInfection and Immunity
Volume64
Issue number6
StatePublished - Jun 1996

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Moraxella (Branhamella) catarrhalis
Lactoferrin
Transferrin
Membrane Proteins
Iron
Growth
Gram-Negative Bacteria
Heme
Amino Acid Sequence
Carrier Proteins
ferric citrate
Proteins

ASJC Scopus subject areas

  • Immunology

Cite this

Aebi, C., Stone, B., Beucher, M., Cope, L. D., Maciver, I., Thomas, S. E., ... Hansen, E. J. (1996). Expression of the CopB outer membrane protein by Moraxella catarrhalis is regulated by iron and affects iron acquisition from transferrin and lactoferrin. Infection and Immunity, 64(6), 2024-2030.

Expression of the CopB outer membrane protein by Moraxella catarrhalis is regulated by iron and affects iron acquisition from transferrin and lactoferrin. / Aebi, Christoph; Stone, Barbara; Beucher, Margaret; Cope, Leslie D.; Maciver, Isobel; Thomas, Sharon E.; Mccracken, George H.; Sparling, P. Frederick; Hansen, Eric J.

In: Infection and Immunity, Vol. 64, No. 6, 06.1996, p. 2024-2030.

Research output: Contribution to journalArticle

Aebi, C, Stone, B, Beucher, M, Cope, LD, Maciver, I, Thomas, SE, Mccracken, GH, Sparling, PF & Hansen, EJ 1996, 'Expression of the CopB outer membrane protein by Moraxella catarrhalis is regulated by iron and affects iron acquisition from transferrin and lactoferrin', Infection and Immunity, vol. 64, no. 6, pp. 2024-2030.
Aebi, Christoph ; Stone, Barbara ; Beucher, Margaret ; Cope, Leslie D. ; Maciver, Isobel ; Thomas, Sharon E. ; Mccracken, George H. ; Sparling, P. Frederick ; Hansen, Eric J. / Expression of the CopB outer membrane protein by Moraxella catarrhalis is regulated by iron and affects iron acquisition from transferrin and lactoferrin. In: Infection and Immunity. 1996 ; Vol. 64, No. 6. pp. 2024-2030.
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abstract = "The amino acid sequence of the cell-surface-exposed, 81-kDa CopB outer membrane protein of Moraxella catarrhalis was found to be similar to those of TonB-dependent outer membrane proteins of other gram-negative bacteria. Expression of CopB was affected by the availability of iron in the growth medium, and the extent of overexpression of CopB in response to iron limitation varied widely among the M. catarrhalis strains tested. Wild-type M. catarrhalis strains were found to be able to utilize ferric citrate, transferrin, lactoferrin, and heme as sources of iron for growth in vitro. However, an isogenic copB mutant was severely impaired in its ability to utilize transferrin and lactoferrin as sole sources of iron for growth, whereas this same mutant grew similarly to the wild-type parent strain when supplied with ferric citrate as the iron source. The copB mutant was not significantly different from its wild-type parent strain in its ability to bind transferrin and lactoferrin. In addition, the wild-type parent strain and the copB mutant exhibited equivalent rates of uptake of 55Fe from ferric citrate. However, the copB mutant was markedly less able than the wild-type strain to take up 55Fe from transferrin and lactoferrin. These results indicate that lack of expression of the CopB protein exerts a direct or indirect effect on the ability of M. catarrhalis to utilize iron bound to certain carrier proteins.",
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