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

2016 ◽  
Vol 198 (24) ◽  
pp. 3265-3277 ◽  
Author(s):  
Pauline Moulin ◽  
Kévin Patron ◽  
Camille Cano ◽  
Mohamed Amine Zorgani ◽  
Emilie Camiade ◽  
...  

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 , 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. IMPORTANCE 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.

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Ryuichi Hirota ◽  
Kenji Abe ◽  
Zen-ichiro Katsuura ◽  
Reiji Noguchi ◽  
Shigeaki Moribe ◽  
...  

2019 ◽  
Vol 201 (8) ◽  
Author(s):  
P. Moulin ◽  
V. Rong ◽  
A. Ribeiro E Silva ◽  
V. G. Pederick ◽  
E. Camiade ◽  
...  

ABSTRACTStreptococcus agalactiaeis not only part of the human intestinal and urogenital microbiota but is also a leading cause of septicemia and meningitis in neonates. Its ability to cause disease depends upon the acquisition of nutrients from its environment, including the transition metal ion zinc. The primary zinc acquisition system of the pathogen is the Adc/Lmb ABC permease, which is essential for viability in zinc-restricted environments. Here, we show that in addition to the AdcCB transporter and the three zinc-binding proteins, Lmb, AdcA, and AdcAII,S. agalactiaezinc homeostasis also involves two streptococcal histidine triad (Sht) proteins. Sht and ShtII are required for zinc uptake via the Lmb and AdcAII proteins with apparent overlapping functionality and specificity. Both Sht-family proteins possess five-histidine triad motifs with similar hierarchies of importance for Zn homeostasis. Independent of its contribution to zinc homeostasis, Sht has previously been reported to bind factor H leading to predictions of a contribution to complement evasion. Here, we investigated ShtII to ascertain whether it had similar properties. Analysis of recombinant Sht and ShtII reveals that both proteins have similar affinities for factor H binding. However, neither protein aided in resistance to complement in human blood. These findings challenge prior inferences regarding thein vivorole of the Sht proteins in resisting complement‐mediated clearance.IMPORTANCEThis study examined the role of the two streptococcal histidine triad (Sht) proteins ofStreptococcus agalactiaein zinc homeostasis and complement resistance. We showed that Sht and ShtII facilitate zinc homeostasis in conjunction with the metal-binding proteins Lmb and AdcAII. Here, we show that the Sht-family proteins are functionally redundant with overlapping roles in zinc uptake. Further, this work reveals that although the Sht-family proteins bind to factor Hin vitrothis did not influence survival in human blood.


2021 ◽  
Vol 337 ◽  
pp. 108928
Author(s):  
Trond Møretrø ◽  
Birgitte Moen ◽  
Valérie L. Almli ◽  
Paula Teixeira ◽  
Vânia B. Ferreira ◽  
...  

2020 ◽  
Vol 99 (6) ◽  
pp. 226-231
Author(s):  
A.V. Permyakova ◽  
◽  
A.V. Sazhin ◽  
E.V. Melekhina ◽  
A.V. Gorelov ◽  
...  

The review presents the existing biological and mathematical models of the infection process caused by the Epstein–Barr virus. The existence of the Epstein–Barr virus in the host organism can be described by a model representing a cycle of six consecutive stages, each of them has its own independent variant of immune regulation. The phenomenon of virus excretion in biological fluids, in particular, in saliva, is modeled using differential equations. Usage of mathematical modeling allows us to supplement existing knowledge about the pathogenesis of the infectious process caused by the Epstein–Barr virus, as well as to determine threshold levels of virus isolation in non-sterile environments for the diagnosis of active forms of infection.


2016 ◽  
Vol 198 (7) ◽  
pp. 1087-1100 ◽  
Author(s):  
Gursonika Binepal ◽  
Kamal Gill ◽  
Paula Crowley ◽  
Martha Cordova ◽  
L. Jeannine Brady ◽  
...  

ABSTRACTPotassium (K+) is the most abundant cation in the fluids of dental biofilm. The biochemical and biophysical functions of K+and a variety of K+transport systems have been studied for most pathogenic bacteria but not for oral pathogens. In this study, we establish the modes of K+acquisition inStreptococcus mutansand the importance of K+homeostasis for its virulence attributes. TheS. mutansgenome harbors four putative K+transport systems that included two Trk-like transporters (designated Trk1 and Trk2), one glutamate/K+cotransporter (GlnQHMP), and a channel-like K+transport system (Kch). Mutants lacking Trk2 had significantly impaired growth, acidogenicity, aciduricity, and biofilm formation. [K+] less than 5 mM eliminated biofilm formation inS. mutans. The functionality of the Trk2 system was confirmed by complementing anEscherichia coliTK2420 mutant strain, which resulted in significant K+accumulation, improved growth, and survival under stress. Taken together, these results suggest that Trk2 is the main facet of the K+-dependent cellular response ofS. mutansto environment stresses.IMPORTANCEBiofilm formation and stress tolerance are important virulence properties of caries-causingStreptococcus mutans. To limit these properties of this bacterium, it is imperative to understand its survival mechanisms. Potassium is the most abundant cation in dental plaque, the natural environment ofS. mutans. K+is known to function in stress tolerance, and bacteria have specialized mechanisms for its uptake. However, there are no reports to identify or characterize specific K+transporters inS. mutans. We identified the most important system for K+homeostasis and its role in the biofilm formation, stress tolerance, and growth. We also show the requirement of environmental K+for the activity of biofilm-forming enzymes, which explains why such high levels of K+would favor biofilm formation.


2012 ◽  
Vol 78 (8) ◽  
pp. 2841-2849 ◽  
Author(s):  
Evan F. Goulden ◽  
Michael R. Hall ◽  
David G. Bourne ◽  
Lily L. Pereg ◽  
Lone Høj

ABSTRACTThe type strain ofVibrio owensii(DY05) was isolated during an epizootic of aquaculture-reared larvae (phyllosomas) of the ornate spiny lobster (Panulirus ornatus).V. owensiiDY05 was formally demonstrated to be the etiological agent of a disease causing rapid and reproducible larval mortality with pathologies similar to those seen during disease epizootics. Vectored challenge via the aquaculture live feed organismArtemia(brine shrimp) caused consistent cumulative mortality rates of 84 to 89% after 72 h, in contrast to variable mortality rates seen after immersion challenge. Histopathological examination of vector-challenged phyllosomas revealed bacterial proliferation in the midgut gland (hepatopancreas) concomitant with epithelial cell necrosis. A fluorescent-protein-labeledV. owensiiDY05 transconjugant showed dispersal of single cells in the foregut and hepatopancreas 6 h postexposure, leading to colonization of the entire hepatopancreas within 18 h and eventually systemic infection.V. owensiiDY05 is a marine enteropathogen highly virulent toP. ornatusphyllosoma that uses vector-mediated transmission and release from host association to a planktonic existence to perpetuate transfer. This understanding of the infection process will improve targeted biocontrol strategies and enhance the prospects of commercially viable larviculture for this valuable spiny lobster species.


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