The fibronectin-binding capacity and host cell adherence of Streptococcus pyogenes strains are discordant with each other

M Edwards, Peter Fagan, Bart Currie, K Sriprakash

    Research output: Contribution to journalArticleResearchpeer-review

    Abstract

    Surface exposed fibronectin-binding proteins (FBPs) play an important role in the adherence of Streptococcus pyogenes (group A streptococcus, GAS) to host cells. This pathogen expresses numerous FBPs, of which SfbI, SfbII and PrtF2 are major surface exposed FBPs. However, GAS strains differ in the genetic potential to express these proteins. To test whether this difference reflects in differences in fibronectin (Fn) binding, a set of circulating strains previously examined for adherence to host cells was used. The 68 distinct strains were isolated from throat, skin and blood. They were analyzed for (a) the presence of genes for SfbI, SfbII and PrtF2 and (b) the extent of Fn binding. The results suggest that strains possessing two or more of the genes for these FBPs bound Fn significantly more than strains possessing none or one of the genes. No correlation between the extent of Fn binding and the tissue site of isolation was found. Furthermore, together with our previous studies on adherence capacity of these GAS strains, we found no correlation between Fn binding ability and the avidity of the strains to adhere to epithelial cells. We suggest that while Fn binding is important for adhesion, for many GAS strains the extent of Fn binding is not the critical determinant of adherence. � 2004 Elsevier SAS. All rights reserved.
    Original languageEnglish
    Pages (from-to)1156-1162
    Number of pages7
    JournalMicrobes and Infection
    Volume6
    Issue number13
    Publication statusPublished - 2004

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    Streptococcus pyogenes
    Fibronectins
    Streptococcus
    Carrier Proteins
    Genes
    Pharynx
    Epithelial Cells
    Binding Sites

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    title = "The fibronectin-binding capacity and host cell adherence of Streptococcus pyogenes strains are discordant with each other",
    abstract = "Surface exposed fibronectin-binding proteins (FBPs) play an important role in the adherence of Streptococcus pyogenes (group A streptococcus, GAS) to host cells. This pathogen expresses numerous FBPs, of which SfbI, SfbII and PrtF2 are major surface exposed FBPs. However, GAS strains differ in the genetic potential to express these proteins. To test whether this difference reflects in differences in fibronectin (Fn) binding, a set of circulating strains previously examined for adherence to host cells was used. The 68 distinct strains were isolated from throat, skin and blood. They were analyzed for (a) the presence of genes for SfbI, SfbII and PrtF2 and (b) the extent of Fn binding. The results suggest that strains possessing two or more of the genes for these FBPs bound Fn significantly more than strains possessing none or one of the genes. No correlation between the extent of Fn binding and the tissue site of isolation was found. Furthermore, together with our previous studies on adherence capacity of these GAS strains, we found no correlation between Fn binding ability and the avidity of the strains to adhere to epithelial cells. We suggest that while Fn binding is important for adhesion, for many GAS strains the extent of Fn binding is not the critical determinant of adherence. � 2004 Elsevier SAS. All rights reserved.",
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    author = "M Edwards and Peter Fagan and Bart Currie and K Sriprakash",
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    language = "English",
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    The fibronectin-binding capacity and host cell adherence of Streptococcus pyogenes strains are discordant with each other. / Edwards, M; Fagan, Peter; Currie, Bart; Sriprakash, K.

    In: Microbes and Infection, Vol. 6, No. 13, 2004, p. 1156-1162.

    Research output: Contribution to journalArticleResearchpeer-review

    TY - JOUR

    T1 - The fibronectin-binding capacity and host cell adherence of Streptococcus pyogenes strains are discordant with each other

    AU - Edwards, M

    AU - Fagan, Peter

    AU - Currie, Bart

    AU - Sriprakash, K

    PY - 2004

    Y1 - 2004

    N2 - Surface exposed fibronectin-binding proteins (FBPs) play an important role in the adherence of Streptococcus pyogenes (group A streptococcus, GAS) to host cells. This pathogen expresses numerous FBPs, of which SfbI, SfbII and PrtF2 are major surface exposed FBPs. However, GAS strains differ in the genetic potential to express these proteins. To test whether this difference reflects in differences in fibronectin (Fn) binding, a set of circulating strains previously examined for adherence to host cells was used. The 68 distinct strains were isolated from throat, skin and blood. They were analyzed for (a) the presence of genes for SfbI, SfbII and PrtF2 and (b) the extent of Fn binding. The results suggest that strains possessing two or more of the genes for these FBPs bound Fn significantly more than strains possessing none or one of the genes. No correlation between the extent of Fn binding and the tissue site of isolation was found. Furthermore, together with our previous studies on adherence capacity of these GAS strains, we found no correlation between Fn binding ability and the avidity of the strains to adhere to epithelial cells. We suggest that while Fn binding is important for adhesion, for many GAS strains the extent of Fn binding is not the critical determinant of adherence. � 2004 Elsevier SAS. All rights reserved.

    AB - Surface exposed fibronectin-binding proteins (FBPs) play an important role in the adherence of Streptococcus pyogenes (group A streptococcus, GAS) to host cells. This pathogen expresses numerous FBPs, of which SfbI, SfbII and PrtF2 are major surface exposed FBPs. However, GAS strains differ in the genetic potential to express these proteins. To test whether this difference reflects in differences in fibronectin (Fn) binding, a set of circulating strains previously examined for adherence to host cells was used. The 68 distinct strains were isolated from throat, skin and blood. They were analyzed for (a) the presence of genes for SfbI, SfbII and PrtF2 and (b) the extent of Fn binding. The results suggest that strains possessing two or more of the genes for these FBPs bound Fn significantly more than strains possessing none or one of the genes. No correlation between the extent of Fn binding and the tissue site of isolation was found. Furthermore, together with our previous studies on adherence capacity of these GAS strains, we found no correlation between Fn binding ability and the avidity of the strains to adhere to epithelial cells. We suggest that while Fn binding is important for adhesion, for many GAS strains the extent of Fn binding is not the critical determinant of adherence. � 2004 Elsevier SAS. All rights reserved.

    KW - binding protein

    KW - fibronectin

    KW - protein subunit

    KW - article

    KW - bacterial strain

    KW - bacterium adherence

    KW - bacterium isolation

    KW - blood

    KW - correlation analysis

    KW - epithelium cell

    KW - host cell

    KW - human

    KW - priority journal

    KW - protein binding

    KW - protein expression

    KW - skin

    KW - Streptococcus pyogenes

    KW - throat

    KW - Adhesins, Bacterial

    KW - Bacterial Adhesion

    KW - Bacterial Proteins

    KW - Blood

    KW - Cell Line

    KW - Cell Line, Tumor

    KW - DNA, Bacterial

    KW - Fibronectins

    KW - Genes, Bacterial

    KW - Humans

    KW - Pharynx

    KW - Protein Binding

    KW - Skin

    KW - Streptococcal Infections

    KW - Streptococcus sp. 'group A'

    M3 - Article

    VL - 6

    SP - 1156

    EP - 1162

    JO - Microbes and Infection

    JF - Microbes and Infection

    SN - 1286-4579

    IS - 13

    ER -