scholarly journals Collagen-binding proteins ofStreptococcus mutansand related streptococci

2016 ◽  
Vol 32 (2) ◽  
pp. 89-106 ◽  
Author(s):  
A. Avilés-Reyes ◽  
J.H. Miller ◽  
J.A. Lemos ◽  
J. Abranches
Keyword(s):  
Binding Proteins ◽  
Collagen Binding

Fluorescently labeled collagen binding proteins allow specific visualization of collagen in tissues and live cell culture

2006 ◽  
Vol 350 (2) ◽  
pp. 177-185 ◽  
Author(s):  
Katy Nash Krahn ◽  
Carlijn V.C. Bouten ◽  
Sjoerd van Tuijl ◽  
Marc A.M.J. van Zandvoort ◽  
Maarten Merkx
Keyword(s):  
Cell Culture ◽  
Binding Proteins ◽  
Live Cell ◽  
Collagen Binding

scholarly journals The FasX Small Regulatory RNA Negatively Regulates the Expression of Two Fibronectin-Binding Proteins in Group A Streptococcus

2015 ◽  
Vol 197 (23) ◽  
pp. 3720-3730 ◽  
Author(s):  
Jessica L. Danger ◽  
Nishanth Makthal ◽  
Muthiah Kumaraswami ◽  
Paul Sumby
Keyword(s):  
Cell Surface ◽  
Virulence Factors ◽  
Binding Proteins ◽  
Mrna Translation ◽  
Regulatory Rna ◽  
Collagen Binding ◽  
Content Type ◽  
Small Regulatory Rna ◽  
Group A ◽  
Fibronectin Binding

ABSTRACTThe group AStreptococcus(GAS;Streptococcus pyogenes) causes more than 700 million human infections each year. The success of this pathogen can be traced in part to the extensive arsenal of virulence factors that are available for expression in temporally and spatially specific manners. To modify the expression of these virulence factors, GAS use both protein- and RNA-based regulators, with the best-characterized RNA-based regulator being the small regulatory RNA (sRNA) FasX. FasX is a 205-nucleotide sRNA that contributes to GAS virulence by enhancing the expression of the thrombolytic secreted virulence factor streptokinase and by repressing the expression of the collagen-binding cell surface pili. Here, we have expanded the FasX regulon, showing that this sRNA also negatively regulates the expression of the adhesion- and internalization-promoting, fibronectin-binding proteins PrtF1 and PrtF2. FasX posttranscriptionally regulates the expression of PrtF1/2 through a mechanism that involves base pairing to theprtF1andprtF2mRNAs within their 5′ untranslated regions, overlapping the mRNA ribosome-binding sites. Thus, duplex formation between FasX and theprtF1andprtF2mRNAs blocks ribosome access, leading to an inhibition of mRNA translation. Given that FasX positively regulates the expression of the spreading factor streptokinase and negatively regulates the expression of the collagen-binding pili and of the fibronectin-binding PrtF1/2, our data are consistent with FasX functioning as a molecular switch that governs the transition of GAS between the colonization and dissemination stages of infection.IMPORTANCEMore than half a million deaths each year are a consequence of infections caused by GAS. Insights into how this pathogen regulates the production of proteins during infection may facilitate the development of novel therapeutic or preventative regimens aimed at inhibiting this activity. Here, we have expanded insight into the regulatory activity of the GAS small RNA FasX. In addition to identifying that FasX reduces the abundance of the cell surface-located fibronectin-binding proteins PrtF1/2, fibronectin is present in high abundance in human tissues, and we have determined the mechanism behind this regulation. Importantly, as FasX is the only mechanistically characterized regulatory RNA in GAS, it serves as a model RNA in this and related pathogens.

Entamoeba histolytica: cDNAs cloned as 30kDa collagen-binding proteins (CBP) belong to an antioxidant molecule family.

2004 ◽  
Vol 108 (1-2) ◽  
pp. 7-17 ◽  
Author(s):  
Bertha Jiménez-Delgadillo ◽  
Partha P. Chaudhuri ◽  
Lidia Baylón-Pacheco ◽  
Aracely López-Monteon ◽  
Patricia Talamás-Rohana ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Binding Proteins ◽  
Collagen Binding ◽  
Antioxidant Molecule

Distribution of Streptococcus mutans strains with collagen-binding proteins in the oral cavity of IgA nephropathy patients

2014 ◽  
Vol 19 (5) ◽  
pp. 844-850 ◽  
Author(s):  
Taro Misaki ◽  
Shuhei Naka ◽  
Keiko Kuroda ◽  
Ryota Nomura ◽  
Tempei Shiooka ◽  
...  
Keyword(s):  
Oral Cavity ◽  
Iga Nephropathy ◽  
Streptococcus Mutans ◽  
Binding Proteins ◽  
Collagen Binding

Purification of collagen-binding proteins ofLactobacillus reuteri NCIB 11951

1994 ◽  
Vol 28 (4) ◽  
pp. 231-236 ◽  
Author(s):  
P. Aleljung ◽  
W. Shen ◽  
B. Rozalska ◽  
U. Hellman ◽  
Å. Ljungh ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Collagen Binding

scholarly journals Isolation and characterization of the neutrophil-binding proteins for platelet-derived adherence-inhibiting factor

Blood ◽  
1993 ◽  
Vol 82 (6) ◽  
pp. 1884-1890 ◽  
Author(s):  
K Iwabuchi ◽  
I Nagaoka ◽  
A Someya ◽  
T Yamashita
Keyword(s):  
Affinity Chromatography ◽  
Binding Sites ◽  
Binding Proteins ◽  
Type Iv Collagen ◽  
Affinity Binding ◽  
Collagen Binding ◽  
Type Iv ◽  
Isolation And Characterization ◽  
Inhibiting Factor ◽  
Sepharose Column

Abstract Guinea pig neutrophils adhered to adherence-inhibiting factor (AIF)- coated plastic; the adherence was completely inhibited by the addition of AIF, but partly inhibited by type IV collagen. Binding of 125I- labeled AIF to neutrophils was inhibited by unlabeled AIF, but partly inhibited by type IV collagen. Scatchard analysis showed that neutrophils have two classes of binding sites for AIF, high-affinity binding sites (kd = 5.0 pmol/L) numbering 500 per cell and low-affinity binding sites (kd = 860 pmol/L) numbering 6,400 per cell. Type IV collagen increased the kd of low-affinity binding sites. We have isolated and characterized the AIF-binding sites. We have isolated and characterized the AIF-binding proteins. Using AIF affinity chromatography, the radioactive fraction containing six proteins of molecular mass 45, 63, 87, 90 to 105, 145, and 195 Kd was isolated from 125I surface-labeled neutrophil extracts. This radioactive fraction was further separated into two fractions using type IV collagen affinity chromatography, ie, one fraction was adsorbed on the type IV collagen column and contained the 45-, 63-, and 87-Kd proteins, whereas another fraction was not adsorbed on the column and contained the 45-, 63-, 90- to 105-, 145-, and 195-Kd proteins. To isolate the type IV collagen- binding proteins, 125I surface-labeled neutrophil extracts were applied to a type IV collagen-Sepharose column; the isolated radioactive fraction contained the 45-, 63-, and 87-Kd proteins and bound to an AIF- Sepharose column. Taken together, these results suggest that the AIF- binding proteins, which bind to type IV collagen, are the type IV collagen-binding proteins of neutrophils.

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