scholarly journals Prevalence of the Amylase-Binding Protein A Gene (abpA) in Oral Streptococci

1999 ◽  
Vol 37 (12) ◽  
pp. 4081-4085 ◽  
Author(s):  
Alan E. Brown ◽  
Jeffrey D. Rogers ◽  
Elaine M. Haase ◽  
Peter M. Zelasko ◽  
Frank A. Scannapieco
Keyword(s):  
Southern Blot ◽  
Genomic Dna ◽  
Binding Protein ◽  
Protein A ◽  
Oral Streptococci ◽  
Streptococcus Anginosus ◽  
Streptococcus Oralis ◽  
Genes Encoding ◽  
Pcr Products ◽  
Streptococcal Species

Salivary amylase binds specifically to a number of oral streptococcal species. This interaction may play an important role in dental plaque formation. Recently, a 585-bp gene was cloned and sequenced from Streptococcus gordonii Challis encoding a 20.5-kDa amylase-binding protein (AbpA). The goal of this study was to determine if related genes are present in other species of oral streptococci. Biotinylated abpA was used in Southern blot analysis to screen genomic DNA from several strains representing eight species of oral streptococci. This probe hybridized with a 4.0-kbHindIII restriction fragment from all 13 strains ofS. gordonii tested. The probe did not appear to bind to any restriction fragments from other species of amylase-binding oral streptococci including Streptococcus mitis (with the exception of 1 of 14 strains), Streptococcus crista (3 strains), Streptococcus anginosus (1 strain), andStreptococcus parasanguinis (1 strain), or to non-amylase-binding oral streptococci including Streptococcus sanguinis (3 strains), Streptococcus oralis (4 strains), and Streptococcus mutans (1 strain). Primers homologous to sequences within the 3′ and 5′ ends of abpAyielded products of 400 bp following PCR of genomic DNA from the Southern blot-positive strains. Several of these PCR products were cloned and sequenced. The levels of similarity of these cloned products to the abpA of S. gordonii Challis ranged from 91 to 96%. These studies reveal that the abpA gene appears to be specific to S. gordonii and differs from genes encoding amylase-binding proteins from other species of amylase-binding streptococci.

scholarly journals Distribution and Genetic Diversity of the ABC Transporter Lipoproteins PiuA and PiaA within Streptococcus pneumoniae and Related Streptococci

2006 ◽  
Vol 188 (3) ◽  
pp. 1031-1038 ◽  
Author(s):  
Rachael H. Whalan ◽  
Simon G. P. Funnell ◽  
Lucas D. Bowler ◽  
Michael J. Hudson ◽  
Andrew Robinson ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Streptococcus Pneumoniae ◽  
Oral Streptococci ◽  
Pneumococcal Infections ◽  
Closely Related Species ◽  
Streptococcus Oralis ◽  
Amino Acid Divergence ◽  
Genes Encoding ◽  
Associated Proteins ◽  
Nucleotide Divergence

ABSTRACT Streptococcus pneumoniae is a major cause of morbidity and mortality worldwide. The existence of approximately 90 antigenically distinct capsular serotypes has greatly complicated the development of an effective pneumococcal vaccine. Virulence-associated proteins common and conserved among all capsular types now represent the best strategy to combat pneumococcal infections. PiuA and PiaA are the lipoprotein components of two pneumococcal iron ABC transporters and are required for full virulence in mouse models of infection. Here we describe a study of the distribution and genetic diversity of PiuA and PiaA within typical and atypical S. pneumoniae, Streptococcus oralis, and Streptococcus mitis strains. The genes encoding both PiuA and PiaA were present in all typical pneumococci tested, (covering 20 and 27 serotypes, respectively). The piuA gene was highly conserved within the typical pneumococci (0.3% nucleotide divergence), but was also present in “atypical” pneumococci and the closely related species S. mitis and S. oralis, showing up to 10.4% nucleotide divergence and 7.5% amino acid divergence from the typical pneumococcal alleles. Conversely, the piaA gene was found to be specific to typical pneumococci, 100% conserved, and absent from the oral streptococci, including isolates of S. mitis known to possess pneumolysin and autolysin. These are desirable qualities for a vaccine candidate and as a diagnostic tool for S. pneumoniae.

scholarly journals Virulence factors in streptococcal infective endocarditis

2005 ◽  
Vol 26 (3) ◽  
pp. 114
Author(s):  
Derek W S Harty
Keyword(s):  
Infective Endocarditis ◽  
Heart Valves ◽  
Blood Stream ◽  
Mutans Streptococci ◽  
Oral Streptococci ◽  
Streptococcus Anginosus ◽  
Streptococcus Oralis ◽  
Causative Agents ◽  
Life Threatening ◽  
Micro Organisms

Infective endocarditis (IE) is a life threatening, endovascular infection occurring when bacteria enter the blood stream and adhere to heart valves. Mortality rates remain in the range of 11-27%. The most common infecting micro-organisms are now the staphylococci (44%) although streptococci (31%) and particularly the oral streptococci (21%) are still major causative agents. Many different oral streptococci have been isolated from IE cases, the most common being Streptococcus sanguinis, Streptococcus oralis, Streptococcus gordonii, Streptococcus mitis, Streptococcus anginosus group and mutans streptococci.

scholarly journals Noncatalytic Docking Domains of Cellulosomes of Anaerobic Fungi

2001 ◽  
Vol 183 (18) ◽  
pp. 5325-5333 ◽  
Author(s):  
Peter J. M. Steenbakkers ◽  
Xin-Liang Li ◽  
Eduardo A. Ximenes ◽  
Jorik G. Arts ◽  
Huizhong Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cdna Library ◽  
Genomic Dna ◽  
Catalytic Domain ◽  
Sequence Information ◽  
Anaerobic Fungi ◽  
Degenerate Primers ◽  
New Genes ◽  
Genes Encoding ◽  
Pcr Products

ABSTRACT A method is presented for the specific isolation of genes encoding cellulosome components from anaerobic fungi. The catalytic components of the cellulosome of anaerobic fungi typically contain, besides the catalytic domain, mostly two copies of a 40-amino-acid cysteine-rich, noncatalytic docking domain (NCDD) interspaced by short linkers. Degenerate primers were designed to anneal to the highly conserved region within the NCDDs of the monocentric fungusPiromyces sp. strain E2 and the polycentric fungusOrpinomyces sp. strain PC-2. Through PCR using cDNA fromOrpinomyces sp. and genomic DNA fromPiromyces sp. as templates, respectively, 9 and 19 PCR products were isolated encoding novel NCDD linker sequences. Screening of an Orpinomyces sp. cDNA library with four of these PCR products resulted in the isolation of new genes encoding cellulosome components. An alignment of the partial NCDD sequence information obtained and an alignment of database-accessible NCDD sequences, focusing on the number and position of cysteine residues, indicated the presence of three structural subfamilies within fungal NCDDs. Furthermore, evidence is presented that the NCDDs in CelC from the polycentric fungus Orpinomyces sp. strain PC-2 specifically recognize four proteins in a cellulosome preparation, indicating the presence of multiple scaffoldins.

scholarly journals Genetic Relationships between Clinical Isolates of Streptococcus pneumoniae, Streptococcus oralis, and Streptococcus mitis: Characterization of “Atypical” Pneumococci and Organisms Allied to S. mitis HarboringS. pneumoniae Virulence Factor-Encoding Genes

2000 ◽  
Vol 68 (3) ◽  
pp. 1374-1382 ◽  
Author(s):  
Adrian M. Whatmore ◽  
Androulla Efstratiou ◽  
A. Paul Pickerill ◽  
Karen Broughton ◽  
Geoffrey Woodard ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Clinical Laboratory ◽  
Genetic Relationships ◽  
Housekeeping Genes ◽  
Virulence Determinants ◽  
Streptococcus Mitis ◽  
Streptococcus Oralis ◽  
Capsule Production ◽  
Genes Encoding ◽  
Streptococcal Species

ABSTRACT The oral streptococcal group (mitis phylogenetic group) currently consists of nine recognized species, although the group has been traditionally difficult to classify, with frequent changes in nomenclature over the years. The pneumococcus (Streptococcus pneumoniae), an important human pathogen, is traditionally distinguished from the most closely related oral streptococcal speciesStreptococcus mitis and Streptococcus oralis on the basis of three differentiating characteristics: optochin susceptibility, bile solubility, and agglutination with antipneumococcal polysaccharide capsule antibodies. However, there are many reports in the literature of pneumococci lacking one or more of these defining characteristics. Sometimes called “atypical” pneumococci, these isolates can be the source of considerable confusion in the clinical laboratory. Little is known to date about the genetic relationships of such organisms with classical S. pneumoniae isolates. Here we describe these relationships based on sequence analysis of housekeeping genes in comparison with previously characterized isolates of S. pneumoniae,S. mitis, and S. oralis. While most pneumococci were found to represent a closely related group these studies identified a subgroup of atypical pneumococcal isolates (bile insoluble and/or “acapsular”) distinct from, though most closely related to, the “typical” pneumococcal isolates. However, a large proportion of isolates, found to be atypical on the basis of capsule reaction alone, did group with typical pneumococci, suggesting that they have either lost capsule production or represent as-yet-unrecognized capsular types. In contrast to typical S. pneumoniae, isolates phenotypically identified as S. mitis and S. oralis, which included isolates previously characterized in taxonomic studies, were genetically diverse. While most of the S. oralis isolates did fall into a well-separated group, S. mitis isolates did not cluster into a well-separated group. During the course of these studies we also identified a number of potentially important pathogenic isolates, which were frequently associated with respiratory disease, that phenotypically and genetically are most closely related to S. mitis but which harbor genes encoding the virulence determinants pneumolysin and autolysin classically associated with S. pneumoniae.

scholarly journals The Effect of Benzyl Isothiocyanate On The Expression of Genes Encoding NADH Oxidase And Fibronectin-Binding Protein In Oral Streptococcal Biofilms

2021 ◽  
Author(s):  
Hawraa Alhandal ◽  
Esraa Almesaileikh ◽  
Radhika G Bhardwaj ◽  
Areej Al Khabbaz ◽  
Maribasappa Karched
Keyword(s):  
Antimicrobial Agent ◽  
Mrna Expression ◽  
Nadh Oxidase ◽  
Binding Protein ◽  
Oral Bacteria ◽  
Oral Streptococci ◽  
Benzyl Isothiocyanate ◽  
Genes Encoding ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Abstract Background: Recent studies have shown that antibiotic treatment results in up- or down regulation of several virulence-associated genes. The genes encoding NADH oxidase (nox) and fibronectin-binding protein (fbp) are known to play important roles in biofilms of some oral bacterial species. The objective was to study the effect of benzyl isothiocyanate (BITC), an antimicrobial agent from Miswak plant, on the expression of nox and fbp genes in some oral streptococci.Methods: Bacterial strains were grown as biofilms in brucella broth. The crystal violet stained biofilms were quantified by optical density measurements at 590 nm. The biofilms were treated with an antimicrobial agent (BITC) for 2 h and fold change in mRNA expression of nox and fbp genes in BITC treated selected oral streptococci was measured by comparative ∆∆Ct method on Real-Time PCR machine.Results: The highest amount of biofilm mass was produced by A. defectiva, followed by S. gordonii, S. mutans, G. elegans and G. adiacens. Upon treatment with BITC, S. gordonii biofilms showed highest mRNA expression for both fbp and nox genes. Mean (SE) folds increase in the expression of nox mRNA: S. gordonii 2 (0.30), followed by S. mutans 1.25 (0.18), A. defectiva 1.03 (0.09), G. adiacens 0.7 (0.03). Similarly for fbp, folds increase in mRNA expression was: S. gordonii 2.65 (0.03), followed by A. defectiva 2.09 (0.60), G. elegans 1.61 (0.40), S. mutans 1.57 (0.20), and G. adiacens 0.58 (0.06). G. elegans mRNA levels for nox were extremely low (0.006-fold). Conclusion: BITC treatment of the biofilms caused an upregulation of biofilm-associated genes fbp and nox genes in most of the tested species suggesting the significance of these genes in biofilm lifestyle of these oral bacteria. Increased expression of nox and fbp genes in the biofilm lifestyle of these species needs further investigation to understand if it contributes to antimicrobial resistance.

Binding of Human Platelet Glycoprotein lb and Actin to Fragments of Actin-Binding Protein

1992 ◽  
Vol 67 (02) ◽  
pp. 252-257 ◽  
Author(s):  
Anne M Aakhus ◽  
J Michael Wilkinson ◽  
Nils Olav Solum
Keyword(s):  
Actin Filaments ◽  
High Speed ◽  
Binding Protein ◽  
Protein A ◽  
Actin Binding ◽  
Platelet Glycoprotein ◽  
Actin Binding Protein ◽  
Crossed Immunoelectrophoresis ◽  
Triton X ◽  
Calpain Inhibitors

SummaryActin-binding protein (ABP) is degraded into fragments of 190 and 90 kDa by calpain. A monoclonal antibody (MAb TI10) against the 90 kDa fragment of ABP coprecipitated with the glycoprotein lb (GP lb) peak observed on crossed immunoelectrophoresis of Triton X-100 extracts of platelets prepared without calpain inhibitors. MAb PM6/317 against the 190 kDa fragment was not coprecipitated with the GP lb peak under such conditions. The 90 kDa fragment was adsorbed on protein A agarose from extracts that had been preincubated with antibodies to GP lb. This supports the idea that the GP Ib-ABP interaction resides in the 90 kDa region of ABP. GP lb was sedimented with the Triton-insoluble actin filaments in trace amounts only, and only after high speed centrifugation (100,000 × g, 3 h). Both the 190 kDa and the 90 kDa fragments of ABP were sedimented with the Triton-insoluble actin filaments.

scholarly journals A Cluster of Cuticle Protein Genes of Drosophila melanogaster at 65A: Sequence, Structure and Evolution

Genetics ◽  
1997 ◽  
Vol 147 (3) ◽  
pp. 1213-1224
Author(s):  
Jean-Philippe Charles ◽  
Carol Chihara ◽  
Shamim Nejad ◽  
Lynn M Riddiford
Keyword(s):  
Drosophila Melanogaster ◽  
Genomic Dna ◽  
Multiple Copy ◽  
Sequence Structure ◽  
Coding Regions ◽  
The Third ◽  
Genetic Complexity ◽  
Genes Encoding ◽  
Cuticle Protein ◽  
Cuticle Proteins

A 36-kb genomic DNA segment of the Drosophila melanogaster genome containing 12 clustered cuticle genes has been mapped and partially sequenced. The cluster maps at 65A 5-6 on the left arm of the third chromosome, in agreement with the previously determined location of a putative cluster encompassing the genes for the third instar larval cuticle proteins LCP5, LCP6 and LCP8. This cluster is the largest cuticle gene cluster discovered to date and shows a number of surprising features that explain in part the genetic complexity of the LCP5, LCP6 and LCP8 loci. The genes encoding LCP5 and LCP8 are multiple copy genes and the presence of extensive similarity in their coding regions gives the first evidence for gene conversion in cuticle genes. In addition, five genes in the cluster are intronless. Four of these five have arisen by retroposition. The other genes in the cluster have a single intron located at an unusual location for insect cuticle genes.

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