2016
DOI: 10.1128/jb.00614-16
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The Adc/Lmb System Mediates Zinc Acquisition in Streptococcus agalactiae and Contributes to Bacterial Growth and Survival

Abstract: 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, ad… Show more

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Cited by 60 publications
(82 citation statements)
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“…However, AdcA has an additional C-terminal ZinT-like domain and the role of the ZinT-like domain of AdcA in GAS homeostasis is yet to be elucidated. Although AdcAII/Lmb and Pht proteins contribute to streptococcal adaptive responses to zinc limitation (Bayle et al, 2011, Moulin et al, 2016, Tedde et al, 2016), the exact mechanisms by which they facilitate zinc acquisition remain unknown. Nevertheless, the significance of the AdcR signaling pathway to GAS pathogenesis is underscored by the observation that inactivation of adcR caused dysregulation of zinc homeostasis and significantly attenuated GAS virulence (Sanson et al, 2015).…”
Section: Introductionmentioning
confidence: 99%
“…However, AdcA has an additional C-terminal ZinT-like domain and the role of the ZinT-like domain of AdcA in GAS homeostasis is yet to be elucidated. Although AdcAII/Lmb and Pht proteins contribute to streptococcal adaptive responses to zinc limitation (Bayle et al, 2011, Moulin et al, 2016, Tedde et al, 2016), the exact mechanisms by which they facilitate zinc acquisition remain unknown. Nevertheless, the significance of the AdcR signaling pathway to GAS pathogenesis is underscored by the observation that inactivation of adcR caused dysregulation of zinc homeostasis and significantly attenuated GAS virulence (Sanson et al, 2015).…”
Section: Introductionmentioning
confidence: 99%
“…Streptococcus agalactiae (group B streptococcus [GBS]) is not only a human commensal of the digestive and genital tracts but also an opportunistic pathogen that causes invasive infections, including septicemia, pneumonia, and meningitis in human neonates (5,6). Zinc acquisition is essential to these processes since our prior studies have established that zinc is required for fundamental processes, including S. agalactiae growth and morphology (7). In S. agalactiae, zinc acquisition involves the AdcCB transporter, which is comprised of the integral membrane protein, AdcB, and the nucleotide binding domain, AdcC.…”
mentioning
confidence: 99%
“…In S. sanguinis SK36, the SSA_0136 and SSA_0137 genes encode components of an Adc zinc ATP-binding cassette (ABC) transporter, which is involved in zinc uptake in several pathogenic streptococci. The SSA_0136 and SSA_0137 genes are called adcC and adcB , respectively (42, 45). The SSA_0260 gene, also termed SsaB ( S. sanguinis adhesin B) (56), is an LraI family lipoprotein and serves as the substrate-binding protein for a Mn/Zn ABC import system (57).…”
Section: Resultsmentioning
confidence: 99%