Identification of a Differentially Expressed Oligopeptide Binding Protein (OppA2) in
            <i>Streptococcus uberis</i>
            by Representational Difference Analysis of cDNA

Taylor, Deborah; Ward, Philip N.; Rapier, Christopher D.; Leigh, James A.; Bowler, Lucas D.

doi:10.1128/jb.185.17.5210-5219.2003

Cited by 21 publications

(17 citation statements)

References 46 publications

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“…For instance, S. uberis synthesizes two binding proteins, and three OBPs are recruited by the Ami transporters of S. pneumoniae or S. thermophilus and by the Hpp system of S. gordonii (2,11,19,35). Moreover, a high level of identity was found between the Opt proteins from L. lactis and the corresponding oligopeptide ABC components of streptococci, suggesting a streptococcal origin of Opt.…”

Section: Discussionmentioning

confidence: 99%

“…The Opt proteins exhibit the highest identities with the corresponding Opp proteins from Streptococcus mutans UA159 (1). Similarly, OptA exhibits higher identities with streptococcal OBPs than with OppA proteins from Lactococcus or Lactobacillus species (4, 27): 48.5, 32.0, 30.0, 31.2, and 28.4% identities were observed with OppA2 from Streptococcus uberis 0140J, AmiA and AliB from Streptococcus pneumoniae R800, HppA from Streptococcus gordonii DL1, and AmiA1 from S. thermophilus St18, respectively (2,11,19,35). OptA (545 aa) and OptS (549 aa) are very short OBPs.…”

Section: Fig 1 Growth Of L Lactis Sk11 and Its Oppmentioning

confidence: 99%

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A Multifunction ABC Transporter (Opt) Contributes to Diversity of Peptide Uptake Specificity within the Genus Lactococcus

et al. 2004

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Growth of Lactococcus lactis in milk depends on the utilization of extracellular peptides. Up to now, oligopeptide uptake was thought to be due only to the ABC transporter Opp. Nevertheless, analysis of several Opp-deficient L. lactis strains revealed the implication of a second oligopeptide ABC transporter, the so-called Opt system. Both transporters are expressed in wild-type strains such as L. lactis SK11 and Wg2, whereas the plasmid-free strains MG1363 and IL-1403 synthesize only Opp and Opt, respectively. The Opt system displays significant differences from the lactococcal Opp system, which made Opt much more closely related to the oligopeptide transporters of streptococci than to the lactococcal Opp system: (i) genetic organization, (ii) peptide uptake specificity, and (iii) presence of two oligopeptide-binding proteins, OptS and OptA. The fact that only OptA is required for nutrition calls into question the function of the second oligopeptide binding protein (Opts). Sequence analysis of oligopeptide-binding proteins from different bacteria prompted us to propose a classification of these proteins in three distinct groups, differentiated by the presence (or not) of precisely located extensions.The ABC transporter family is characterized by a high affinity for their substrates, and it uses ATP hydrolysis to drive a unidirectional accumulation of solutes into the bacterial cytoplasm. A structural similarity of five proteins is generally observed (10). The substrate-binding protein specifically captures the substrate and is therefore considered one of the determinants of transport specificity (5). The binding protein is located in the periplasm of gram-negative bacteria. In gram-positive bacteria, it is present as a lipoprotein anchored to the cell membrane via an N-terminal moiety. The structure of the protein consists of three distinct domains. Two distinct lobes are connected by a flexible hinge (29), which allows two different conformations: an open, unliganded form with a high affinity for the substrate, and a closed, liganded state, in which the substrate is entrapped into the binding protein (the socalled Venus flytrap model). The closed liganded state is characterized by a low affinity for the substrate. The closed liganded binding protein delivers the substrate to the translocon, which consists of two integral transmembrane proteins and two ATP-binding proteins located on the cytoplasmic side of the membrane. According to a recent model (38), a consequence of the substrate binding would be the transmission of a signal to the ATP subunits of the ABC system. This signal results in an increased affinity of the ATP-binding proteins for ATP, which in turn leads to the opening of the transmembrane channel and the simultaneous release of the solute from the binding protein to the opened pore (6).In gram-positive bacteria, uptake of peptides by ABC transport systems is involved in nitrogen nutrition of the organism, as has been well established for lactic acid bacteria, for instance (11,22), or in the regula...

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Section: Discussionmentioning

confidence: 99%

Section: Fig 1 Growth Of L Lactis Sk11 and Its Oppmentioning

confidence: 99%

A Multifunction ABC Transporter (Opt) Contributes to Diversity of Peptide Uptake Specificity within the Genus Lactococcus

et al. 2004

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“…2a and b). Changes in transcriptional expression between 8-h planktonic cells and 8-h biofilm cells as well as 8-h biofilm and 36-h biofilm cells were calculated by the comparative threshold cycle (⌬⌬C T ) method (15,21) and plotted as the fold change in mRNA expression levels.…”

Section: Vol 77 2011 Differential Protein Expression Of S Uberis Bmentioning

confidence: 99%

Differential Protein Expression in Streptococcus uberis under Planktonic and Biofilm Growth Conditions

Crowley

Leigh

Ward

et al. 2011

Appl Environ Microbiol

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The bovine pathogen Streptococcus uberis was assessed for biofilm growth. The transition from planktonic to biofilm growth in strain 0140J correlated with an upregulation of several gene products that have been shown to be important for pathogenesis, including a glutamine ABC transporter (SUB1152) and a lactoferrin binding protein (gene lbp; protein SUB0145).Approximately 33% of bovine mastitis cases within the United Kingdom are attributable to Streptococcus uberis, and infections can be both persistent and resistant to antimicrobial treatment (10,17). In this study, we assess the ability of S. uberis to form biofilms in vitro. We also analyze the S. uberis clinical isolate 0140J under planktonic and biofilm growth conditions in vitro by using gel electrophoresis liquid chromatography (GeLC)-tandem mass spectrometry (MS/MS) and demonstrate that the changes that 0140J undergoes in the transition from planktonic to biofilm growth include factors strongly implicated in pathogenesis.Biofilm formation by S. uberis isolates. To establish biofilm formation among different strains of S. uberis, we analyzed S. uberis isolates 0140J (a strain of high virulence for the lactating bovine mammary gland), EF20, Y38, C197C, C221, and C198 (a strain obtained from a healthy bovine mammary gland and not associated with pathogenesis) (see Table S1 in the supplemental material) in TSBM medium {tryptic soy broth without dextrose [Difco Labs], supplemented with 10 mM PIPES [piperazine-N,NЈ-bis(2-ethanesulfonic acid)], pH 6.6, and 20% [vol/vol] sterile skim milk}, using a microtiter plate biofilm formation assay (4). All isolates formed biofilms in vitro, with C198 forming the smallest biomass (Fig. 1).A previously elucidated difference between strain C198 and all other strains tested is that C198 lacks the hasAB gene cluster and is, as a consequence, acapsular (J. Leigh, personal communication). In support of capsule production being involved in 0140J biofilm growth in vitro, S. uberis capsule size has been shown to increase in the presence of bovine milkrelated constituents (12) and the addition of 20% (vol/vol) bovine milk to medium was found to promote 0140J biofilm formation in vitro (data not shown). Biofilms were grown in tube reactors (1) that were initially inoculated with S. uberis strain 0140J in TSBM for 1 h under no-flow conditions. Both biofilm and planktonic cells were grown at 37°C in TSB supplemented with 10% (vol/vol) lactose (46 g/liter). Protein extraction was carried out essentially as previously described (6). Protein samples (30 ng) were loaded onto 10% acrylamide gels (Protean III system; Bio-Rad) and stained (GelCode blue; Pierce) according to manufacturer's instructions. Gel lanes were cut into 13 to 15 equal-size gel Differential proteomic analysis of

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“…PCR amplification was carried out on DNA from pools of 96 mutants representing a single microtiter tray from an S. uberis strain 0140J pGh9 ϩ ::ISS1 mutant bank, comprised of 8,800 individual clones (39). A screen for ISS1 insertions at a specific locus was carried out by PCR using paired ISS1 and gene-specific primers as first described by Taylor et al (39).…”

Section: Identification Of Lipoprotein Sequences By Pattern Searchingmentioning

confidence: 99%

Lipoprotein Signal Peptides Are Processed by Lsp and Eep of Streptococcus uberis

2008

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Identification of a Differentially Expressed Oligopeptide Binding Protein (OppA2) in Streptococcus uberis by Representational Difference Analysis of cDNA

Cited by 21 publications

References 46 publications

A Multifunction ABC Transporter (Opt) Contributes to Diversity of Peptide Uptake Specificity within the Genus Lactococcus

A Multifunction ABC Transporter (Opt) Contributes to Diversity of Peptide Uptake Specificity within the Genus Lactococcus

Differential Protein Expression in Streptococcus uberis under Planktonic and Biofilm Growth Conditions

Lipoprotein Signal Peptides Are Processed by Lsp and Eep of Streptococcus uberis

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