scholarly journals Selection and characterization of cell binding and internalizing phage antibodies

2012 ◽  
Vol 526 (2) ◽  
pp. 107-113 ◽  
Author(s):  
Yu Zhou ◽  
Lequn Zhao ◽  
James D. Marks
Keyword(s):  
Cell Binding ◽  
Phage Antibodies

scholarly journals Characterization of Selectin-Mediated Cell Binding in Shear Flow Using Micropatterning Technology and Modeling

2010 ◽  
Vol 98 (3) ◽  
pp. 245a
Author(s):  
Konstantinos Konstantopolous ◽  
ZiQiu Tong ◽  
Luthur Siu-Lun Cheung
Keyword(s):  
Shear Flow ◽  
Cell Binding

scholarly journals Fibronectin receptors of phagocytes. Characterization of the Arg-Gly-Asp binding proteins of human monocytes and polymorphonuclear leukocytes.

1988 ◽  
Vol 167 (3) ◽  
pp. 777-793 ◽  
Author(s):  
E J Brown ◽  
J L Goodwin
Keyword(s):  
Surface Molecule ◽  
Human Monocytes ◽  
Ligand Specificity ◽  
Cell Binding ◽  
Antigenic Analysis ◽  
Vitronectin Receptor ◽  
Surface Molecules ◽  
Rgd Sequence ◽  
Single Receptor

We have defined the cell surface molecules of human monocytes and PMN that bind to the chymotryptic cell binding domain of Fn and to a synthetic peptide, KYAVTGRGDS, based on the sequence of Fn, by affinity chromatography. Monocytes express two receptors that differ in their affinity for CBD-Sepharose and peptide-Sepharose, but that both recognize the RGD sequence. Only a single receptor is purified from PMN, which resembles the monocyte surface molecule that binds to peptide-Sepharose. These receptors are not part of the Mac-1, LFA-1, p(150,95) family, but do have homology to the platelet Fn receptor, gpIIb/IIIa. Interestingly, the antigenic crossreactivity between gpIIb/IIIa and the phagocyte receptors purified on peptide-Sepharose is largely in the beta chain of the receptors. The alpha chains appear to be distinct, based on molecular weight, antigenic analysis, and ligand specificity. This receptor also seems to be the surface molecule on monocytes that is critical for phagocytosis enhancement by Fn. Thus, we have defined the phagocyte Fn receptor that transduces the signal for increased phagocytosis by monocytes; it may be a third member of a family of adhesion molecules that includes the gpIIb/IIIa of platelets and the vitronectin receptor of fibroblasts.

scholarly journals Fibronectin dependent macrophage fibrin binding

Blood ◽  
1991 ◽  
Vol 78 (11) ◽  
pp. 2900-2907
Author(s):  
SD Blystone ◽  
LK Weston ◽  
JE Kaplan
Keyword(s):  
Synthetic Peptides ◽  
Cellular Response ◽  
Fluid Phase ◽  
Binding Domain ◽  
Amino Terminus ◽  
Cell Binding ◽  
Fibronectin Fragments ◽  
Cell Binding Domain

Plasma fibronectin has been shown to increase the binding of fibrin monomer to macrophages in vitro. In the present study we began characterization of the mechanism underlying this fibronectin activity. Fragments of fibronectin containing the amino terminus enhanced macrophage fibrin binding to the same extent as intact fibronectin on an equimolar basis. However, fibronectin fragments containing the gelatin-binding domain or the cell-binding domain, but lacking the amino terminus, had no effect on fibrin binding. Fibronectin enhanced fibrin binding was not affected by the addition of synthetic peptides containing the RGD adhesion sequence. The ability of fibronectin to augment fibrin binding remained after paraformaldehyde fixation of macrophage monolayers. Fixation did not alter the basal levels of fibrin binding by macrophages. Preincubation of macrophages with exogenous fibronectin did not increase the binding of fibrin. Fibronectin enhanced fibrin binding remained unaltered after the removal of endogenous cell surface fibronectin by capping with F(ab')2 fragments of antibodies to fibronectin. These results suggest that the amino terminus of fibronectin supports the attachment of fibrin to macrophages by an initial fluid-phase interaction that precedes cellular binding and does not require a cellular response.

scholarly journals Development and structural characterization of a two-MAb cocktail for delayed treatment of enterovirus D68 infections

2020 ◽  
Author(s):  
Zhong Huang ◽  
Chao Zhang ◽  
Cong Xu ◽  
Wenlong Dai ◽  
Yifan Wang ◽  
...  
Keyword(s):  
Therapeutic Agent ◽  
Cell Binding ◽  
Delayed Treatment ◽  
Acute Flaccid Myelitis ◽  
Virus Like Particle ◽  
Enterovirus D68 ◽  
Different Strains ◽  
Further Development ◽  
Potent Neutralization

Abstract Enterovirus D68 (EV-D68) is an emerging pathogen associated with respiratory diseases and/or acute flaccid myelitis. Here, two MAbs, 2H12 and 8F12, raised against EV-D68 virus-like particle (VLP), showed distinct preference in binding VLP and virion and in neutralizing different strains. The 2H12/8F12 cocktail exhibited balanced and potent neutralization effects and conferred broader protection in mice than single MAbs when given at onset of symptoms. Cryo-EM structures of EV-D68 virion complexed with 2H12 or 8F12 showed that both antibodies bind to south rim of the canyon and obscure the canyon, blocking virus–cell binding. Additionally, 2H12 binding could partially impair virions and trigger uncoating, resulting in premature viral RNA release. We also captured an uncoating intermediate induced by 2H12 binding, not detected before in picornaviruses. Our study elucidates neutralizing mechanisms of the MAbs and supports further development of the 2H12/8F12 cocktail as a broad-spectrum therapeutic agent against EV-D68 infections in humans.

scholarly journals Bioinks for 3D Bioprinting: A Scientometric Analysis of Two Decades of Progress

2021 ◽  
Vol 7 (2) ◽  
Author(s):  
Sara Cristina Pedroza-González ◽  
Marisela Rodriguez-Salvador ◽  
Baruc Emet Pérez Benítez ◽  
Mario Moisés Alvarez ◽  
Grissel Trujillo-de Santiago
Keyword(s):  
Biomedical Applications ◽  
Cell Attachment ◽  
Cell Types ◽  
Scientometric Analysis ◽  
Binding Motif ◽  
3D Bioprinting ◽  
Cell Binding ◽  
Biological Performance ◽  
The Cost

This scientometric analysis of 393 original papers published from January 2000 to June 2019 describes the development and use of bioinks for 3D bioprinting. The main trends for bioink applications and the primary considerations guiding the selection and design of current bioink components (i.e., cell types, hydrogels, and additives) were reviewed. The cost, availability, practicality, and basic biological considerations (e.g., cytocompatibility and cell attachment) are the most popular parameters guiding bioink use and development. Today, extrusion bioprinting is the most widely used bioprinting technique. The most reported use of bioinks is the generic characterization of bioink formulations or bioprinting technologies (32%), followed by cartilage bioprinting applications (16%). Similarly, the cell-type choice is mostly generic, as cells are typically used as models to assess bioink formulations or new bioprinting methodologies rather than to fabricate specific tissues. The cell-binding motif arginine-glycine-aspartate is the most common bioink additive. Many articles reported the development of advanced functional bioinks for specific biomedical applications; however, most bioinks remain the basic compositions that meet the simple criteria: Manufacturability and essential biological performance. Alginate and gelatin methacryloyl are the most popular hydrogels that meet these criteria. Our analysis suggests that present-day bioinks still represent a stage of emergence of bioprinting technology.

scholarly journals Fibronectin dependent macrophage fibrin binding

Blood ◽  
1991 ◽  
Vol 78 (11) ◽  
pp. 2900-2907 ◽  
Author(s):  
SD Blystone ◽  
LK Weston ◽  
JE Kaplan
Keyword(s):  
Synthetic Peptides ◽  
Cellular Response ◽  
Fluid Phase ◽  
Binding Domain ◽  
Amino Terminus ◽  
Cell Binding ◽  
Fibronectin Fragments ◽  
Cell Binding Domain

Abstract Plasma fibronectin has been shown to increase the binding of fibrin monomer to macrophages in vitro. In the present study we began characterization of the mechanism underlying this fibronectin activity. Fragments of fibronectin containing the amino terminus enhanced macrophage fibrin binding to the same extent as intact fibronectin on an equimolar basis. However, fibronectin fragments containing the gelatin-binding domain or the cell-binding domain, but lacking the amino terminus, had no effect on fibrin binding. Fibronectin enhanced fibrin binding was not affected by the addition of synthetic peptides containing the RGD adhesion sequence. The ability of fibronectin to augment fibrin binding remained after paraformaldehyde fixation of macrophage monolayers. Fixation did not alter the basal levels of fibrin binding by macrophages. Preincubation of macrophages with exogenous fibronectin did not increase the binding of fibrin. Fibronectin enhanced fibrin binding remained unaltered after the removal of endogenous cell surface fibronectin by capping with F(ab')2 fragments of antibodies to fibronectin. These results suggest that the amino terminus of fibronectin supports the attachment of fibrin to macrophages by an initial fluid-phase interaction that precedes cellular binding and does not require a cellular response.

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