The Adc/Lmb System Mediates Zinc Acquisition in Streptococcus agalactiae and Contributes to Bacterial Growth and Survival
Author(s) -
Pauline Moulin,
Kévin Patron,
Camille Cano,
Mohamed A. Zorgani,
Émilie Camiade,
Elise BorezéeDurant,
Agnès Rosenau,
Laurent Méreghetti,
Aurélia Hiron
Publication year - 2016
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.00614-16
Subject(s) - streptococcus agalactiae , biology , zinc , transporter , microbiology and biotechnology , extracellular , atp binding cassette transporter , translocon , bacterial adhesin , bacteria , biochemistry , streptococcus , gene , membrane protein , escherichia coli , chemistry , genetics , membrane , organic chemistry
The Lmb protein of Streptococcus agalactiae is described as an adhesin that binds laminin, a component of the human extracellular matrix. In this study, we revealed a new role for this protein in zinc uptake. We also identified two Lmb homologs, AdcA and AdcAII, redundant binding proteins that combine with the AdcCB translocon to form a zinc-ABC transporter. Expression of this transporter is controlled by the zinc concentration in the medium through the zinc-dependent regulator AdcR. Triple deletion of lmb, adcA, and adcAII, or that of the adcCB genes, impaired growth and cell separation in a zinc-restricted environment. Moreover, we found that this Adc zinc-ABC transporter promotes S. agalactiae growth and survival in some human biological fluids, suggesting that it contributes to the infection process. These results indicated that zinc has biologically vital functions in S. agalactiae and that, under the conditions tested, the Adc/Lmb transporter constitutes the main zinc acquisition system of the bacterium.
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