The staphylococcal elastin-binding protein regulates zinc-dependent growth/biofilm formation

2014 ◽  
Vol 156 (3) ◽  
pp. 155-162 ◽  
Author(s):  
Makoto Nakakido ◽  
Chihiro Aikawa ◽  
Ichiro Nakagawa ◽  
Kouhei Tsumoto
Keyword(s):  
Biofilm Formation ◽  
Binding Protein ◽  
Elastin Binding Protein ◽  
Dependent Growth

Immunolocalization of 67 kDa elastin-binding protein in perinatal rat lungs

1992 ◽  
Vol 268 (2) ◽  
pp. 277-281 ◽  
Author(s):  
Kojiro Wasano ◽  
Yasuhiro Hirakawa ◽  
Keiichiro Nakamura
Keyword(s):  
Binding Protein ◽  
Rat Lungs ◽  
Elastin Binding Protein

scholarly journals Interaction between the Elastin Peptide VGVAPG and Human Elastin Binding Protein

2012 ◽  
Vol 288 (2) ◽  
pp. 1317-1328 ◽  
Author(s):  
Charlotte Blanchevoye ◽  
Nicolas Floquet ◽  
Amandine Scandolera ◽  
Stéphanie Baud ◽  
Pascal Maurice ◽  
...  
Keyword(s):  
Binding Protein ◽  
Elastin Binding Protein

scholarly journals Molecular Investigation of Fibronectin-Binding Protein Genes and Capacity of Biofilm Production in Staphylococcus Aureus Isolated From Clinical Samples

2021 ◽  
Author(s):  
Hossein Jafari Soghondicolaei ◽  
Mohammad Ahanjan ◽  
Mehrdad Gholami ◽  
Bahman Mirzaei ◽  
Hamid Reza Goli
Keyword(s):  
Staphylococcus Aureus ◽  
Biofilm Formation ◽  
Colorimetric Assay ◽  
Binding Protein ◽  
Clinical Isolates ◽  
Diffusion Method ◽  
Clinical Samples ◽  
Biofilm Production ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Abstract Biofilm production increases Staphylococcus aureus resistance to antibiotics and also host defense mechanisms. The current study aims to evaluate the biofilm formation by S. aureus and to determine the prevalence of fibronectin-binding protein genes, also its correlation with drug resistance. In this study, 100 clinical isolates of S. aureus were collected. The antibiotic susceptibility pattern of the isolates was evaluated by the disk agar diffusion method. The ability of biofilm formation in the studied isolates was also determined by microplate colorimetric assay. Then, all isolates were screened by polymerase chain reaction for the fnbA and fnbB genes. Out of 100 clinical isolates of S. aureus, the highest and lowest antibiotic resistance rates were against penicillin (94%) and vancomycin (6%). Thirty-two cases were found to be multi-drug resistant (MDR) among the all strains. The ability of biofilm production was observed in 89% of the isolates. The PCR results showed that the prevalence of fnbA and fnbB genes were 91% and 17%, respectively. Moreover, 100% and 21.8% of the MDR strains harbored the fnbA and fnbB genes respectively. The ability to form biofilm in MDR isolates of S. aureus is more than non-MDR isolates, especially fnbA positive ones. As the bacteria in the biofilm are difficult to kill by antibiotics, attention to the removal or control of the biofilm production seems to be necessary.

scholarly journals Primary and Secondary Elastin-Binding Protein Defect Leads to Impaired Elastogenesis in Fibroblasts from GM1-Gangliosidosis Patients

2005 ◽  
Vol 167 (6) ◽  
pp. 1689-1698 ◽  
Author(s):  
Anna Caciotti ◽  
Maria Alice Donati ◽  
Tiziana Bardelli ◽  
Alessandra d'Azzo ◽  
Graziella Massai ◽  
...  
Keyword(s):  
Binding Protein ◽  
Gm1 Gangliosidosis ◽  
Elastin Binding Protein

Deletion of penicillin-binding protein 1b impairs biofilm formation and motility in Escherichia coli

2012 ◽  
Vol 163 (4) ◽  
pp. 254-257 ◽  
Author(s):  
Akash Kumar ◽  
Sujoy K. Sarkar ◽  
Dipankar Ghosh ◽  
Anindya S. Ghosh
Keyword(s):  
Escherichia Coli ◽  
Biofilm Formation ◽  
Binding Protein ◽  
Penicillin Binding Protein

Fibulin-5 is an elastin-binding protein essential for elastic fibre development in vivo

Nature ◽  
2002 ◽  
Vol 415 (6868) ◽  
pp. 168-171 ◽  
Author(s):  
Hiromi Yanagisawa ◽  
Elaine C. Davis ◽  
Barry C. Starcher ◽  
Takashi Ouchi ◽  
Masashi Yanagisawa ◽  
...  
Keyword(s):  
Binding Protein ◽  
Elastic Fibre ◽  
Fibre Development ◽  
Elastin Binding Protein

scholarly journals 67-kD elastin-binding protein is a protective "companion" of extracellular insoluble elastin and intracellular tropoelastin.

1994 ◽  
Vol 126 (2) ◽  
pp. 563-574 ◽  
Author(s):  
A Hinek ◽  
M Rabinovitch
Keyword(s):  
Binding Protein ◽  
Light And Electron Microscopy ◽  
Serine Proteinase ◽  
Elastic Fibers ◽  
Fiber Assembly ◽  
Elastin Fiber ◽  
Alternatively Spliced ◽  
Elastin Binding Protein ◽  
Highly Hydrophobic

The 67-kD elastin-binding protein (EBP) mediates cell adhesion to elastin and elastin fiber assembly, and it is similar, if not identical, to the 67-kD enzymatically inactive, alternatively spliced beta-galactosidase. The latter contains an elastin binding domain (S-GAL) homologous both to the aorta EBP and to NH2-terminal sequences of serine proteinases (Hinek, A., M. Rabinovitch, F. W. Keeley, and J. Callahan. 1993. J. Clin. Invest. 91:1198-1205). We now confirm the functional importance of this homology by showing that elastolytic activity of a representative serine elastase, porcine pancreatic elastase, was prevented by an antibody (anti-S-GAL) and by competing with purified EBP or S-GAL peptide. Immunohistochemistry of adult aorta indicates that the EBP exists as a permanent component of mature elastic fibers. This observation, together with the in vitro studies, suggests that the EBP could protect insoluble elastin from extracellular proteolysis and contribute to the extraordinary stability of this protein. Double immunolabeling of fetal lamb aorta with anti-S-GAL and antitropoelastin antibodies demonstrated, under light and electron microscopy, intracellular colocalization of the proteins in smooth muscle cells (SMC). Incubation of SMC with galactosugars to dissociate tropoelastin from EBP caused intracellular aggregation of tropoelastin. A tropoelastin/EBP complex was extracted from SMC lysates by coimmunoprecipitation and cross-linking, and its functional significance was addressed by showing that its dissociation by galactosugars caused degradation of tropoelastin by endogenous serine proteinase(s). This suggests that the EBP may also serve as a "companion" to intracellular tropoelastin, protecting this highly hydrophobic protein from self-aggregation and proteolytic degradation.

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