Vitronectin and type-I collagen binding by Staphylococcus aureus and coagulase-negative staphylococci

Paulsson, M

doi:10.1016/0378-1097(90)90759-j

Cited by 16 publications

(25 citation statements)

References 25 publications

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“…Vitronectins are family of proteins utilized as specific receptors by different pathogenic bacteria in mammalian cells (e.g. Paulsson and Wadstrom, 1990). Because attachment of Agrobacterium cells to plant tissues could be inhibited by human vitronectin or anti‐vitronectin antibodies and because Agrobacterium mutants, which are defective in their attachment ability to plant cells, showed reduced binding to vitronectin, plant vitronectin‐like molecules have been suggested to play a role in Agrobacterium attachment to its host cells (Wagner and Matthysse, 1992); to date, however, no additional progress has been made in the studies of this putative vitronectin‐like plant receptor for Agrobacterium .…”

Section: Plant Cell Surface Receptors and Agrobacterium Attachmentmentioning

confidence: 99%

Biological systems of the host cell involved in Agrobacterium infection

Citovsky¹,

Kozlovsky²,

Lacroix³

et al. 2007

Cell Microbiol

137

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SummaryGenetic transformation of plants by Agrobacterium, which in nature causes neoplastic growths, represents the only known case of trans-kingdom DNA transfer. Furthermore, under laboratory conditions, Agrobacterium can also transform a wide range of other eukaryotic species, from fungi to sea urchins to human cells. How can the Agrobacterium virulence machinery function in such a variety of evolutionarily distant and diverse species? The answer to this question lies in the ability of Agrobacterium to hijack fundamental cellular processes which are shared by most eukaryotic organisms. Our knowledge of these host cellular functions is critical for understanding the molecular mechanisms that underlie genetic transformation of eukaryotic cells. This review outlines the bacterial virulence machinery and provides a detailed discussion of seven major biological systems of the host cell-cell surface receptor arrays, cellular motors, nuclear import, chromatin targeting, targeted proteolysis, DNA repair, and plant immunity -thought to participate in the Agrobacteriummediated genetic transformation.

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Section: Plant Cell Surface Receptors and Agrobacterium Attachmentmentioning

confidence: 99%

Biological systems of the host cell involved in Agrobacterium infection

Citovsky¹,

Kozlovsky²,

Lacroix³

et al. 2007

Cell Microbiol

137

View full text Add to dashboard Cite

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“…One such surface receptor may belong to a vitronectin protein family. In animal cells, vitronectin, a component of the extracellular matrix, is utilized as a specific receptor by several pathogenic bacterial strains ( Paulsson and Wadstrom, 1990). Similarly, plant vitronectin‐like molecules might be involved in the A. tumefaciens –plant cell binding.…”

Section: Introductionmentioning

confidence: 99%

From host recognition to T‐DNA integration: the function of bacterial and plant genes in the Agrobacterium–plant cell interaction

Tzfira

Citovsky

2000

Molecular Plant Pathology

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One of the widest host ranges known among plant pathogens; can potentially attack all dicotyledonous plant species. Also, under controlled conditions (usually in tissue culture), can infect, albeit with lower efficiency, several monocotyledonous species. Agronomic importance: The disease currently affects plants belonging to the rose family, e.g. apple, pear, peach, cherry, almond, roses, as well as poplar trees (aspen). Useful web site:http://www.bio.purdue.edu/courses/gelvinweb/gelvin.html.

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“…5.2%) (Table 1). Other strains bound clusterin lower than 5%, which is considered as negative [19]. Calcium (0.1 mM CaCl 2 ) and magnesium (0.05 mM MgCl 2 ) added to the reaction solution (PBSB) increased the binding of Cowan I slightly, but did not influence the binding of S. epidermidis strains (data not shown).…”

Section: Resultsmentioning

confidence: 96%

“…Clusterin (50 μg) was labelled with Na 125 I (Amersham Plc., Little Chalfron, UK) using a modified chloramine‐T method with Iodobeads (Pierce Chemicals Co., Rockford, IL, USA) [19]. During binding experiments, labelled protein diluted to approx.…”

Section: Methodsmentioning

confidence: 99%

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Binding of human clusterin byStaphylococcus epidermidis

Ljungh

2001

FEMS Immunology &Amp; Medical Microbiology

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To hypothesise that Staphylococcus epidermidis may possess clusterin receptor(s), bacterial binding of human clusterin was determined. In a fluid phase, the binding was markedly influenced by culture medium and three out of 12 S. epidermidis strains grown on ISO-sensitest agar expressed clusterin-binding ability. S. epidermidis J9P, selected for further study, showed saturable binding of iodine-labelled clusterin, and the binding was only inhibited by unlabelled clusterin. The binding was sensitive to protease treatment. Scatchard plot indicated one single class of binding sites (K(d)=104.2 nM). None of the S. epidermidis strains bound immobilised clusterin. These data imply that ligand-receptor interaction exists between S. epidermidis and clusterin in fluid phase, but the domain(s) recognised by bacteria may have been occluded when clusterin was adsorbed on a surface.

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Vitronectin and type-I collagen binding by Staphylococcus aureus and coagulase-negative staphylococci

Cited by 16 publications

References 25 publications

Biological systems of the host cell involved in Agrobacterium infection

Biological systems of the host cell involved in Agrobacterium infection

From host recognition to T‐DNA integration: the function of bacterial and plant genes in the Agrobacterium–plant cell interaction

Binding of human clusterin byStaphylococcus epidermidis

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