The Adc/Lmb System Mediates Zinc Acquisition in Streptococcus agalactiae and Contributes to Bacterial Growth and Survival.
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.



A zinc transporter, composed of three redundant binding proteins (Lmb, AdcA, and AdcAII), was characterized in Streptococcus agalactiae This system was shown to be essential for bacterial growth and morphology in zinc-restricted environments, including human biological fluids.
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France.
Pauline
P
Moulin
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France.
Kévin
K
Patron
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France.
Camille
C
Cano
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France.
Mohamed Amine
MA
Zorgani
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France.
Emilie
E
Camiade
Micalis institute, AgroParis Tech, Université Paris-Saclay, Jouy en Josas, France.
Elise
E
Borezée-Durant
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France.|CHRU de Tours, Service de Bactériologie-Virologie et Hygiène, Tours, France.
Agnès
A
Rosenau
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France.|CHRU de Tours, Service de Bactériologie-Virologie et Hygiène, Tours, France.
Laurent
L
Mereghetti
ISP, Université François Rabelais Tours, INRA, UMR1282, Tours, France aurelia.hiron@univ-tours.fr.
Aurélia
A
Hiron
D018528:ATP-Binding Cassette Transporters / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D015964:Gene Expression Regulation, Bacterial; D050296:Microbial Viability; D013292:Streptococcus agalactiae / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; C114936:AdcA protein, Streptococcus; D001426:Bacterial Proteins; D015032:Zinc
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