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Journal articles on the topic 'RGD motif'

Author: Grafiati

Published: 24 April 2022

Last updated: 30 July 2025

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1

WATTAM, Beth, Dazhuang SHANG, Salman RAHMAN та ін. "Arg-Tyr-Asp (RYD) and Arg-Cys-Asp (RCD) motifs in dendroaspin promote selective inhibition of β1 and β3 integrins". Biochemical Journal 356, № 1 (2001): 11–17. http://dx.doi.org/10.1042/bj3560011.

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Arg-Gly-Asp (RGD) is a unique minimal integrin-binding sequence that is found within several glycoprotein ligands. This sequence has also been found in snake-venom anti-platelet proteins, including the disintegrins and dendroaspin, a natural variant of short-chain neurotoxins isolated from the venom of Dendroaspis jamesonii. In the present study, the motifs RYD and RCD were introduced into the dendroaspin scaffold to replace RGD. Both motifs in dendroaspin caused inhibition of ADP-induced platelet aggregation with IC50 values of 200 and 300nM respectively, similar to that of the wild-type RGD

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2

Davaanyam, Dashdulam, Il-Doo Kim, and Ja-Kyeong Lee. "Intranasal Delivery of RGD-Containing Osteopontin Heptamer Peptide Confers Neuroprotection in the Ischemic Brain and Augments Microglia M2 Polarization." International Journal of Molecular Sciences 22, no. 18 (2021): 9999. http://dx.doi.org/10.3390/ijms22189999.

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Osteopontin (OPN), a phosphorylated glycoprotein, is induced in response to tissue damage and inflammation in various organs, including the brain. In our previous studies, we reported the robust neuroprotective effects of the icosamer OPN peptide OPNpt20, containing arginine-glycine-aspartic acid (RGD) and serine-leucine-alanine-tyrosine (SLAY) motifs, in an animal model of transient focal ischemia and demonstrated that its anti-inflammatory, pro-angiogenic, and phagocytosis inducing functions are responsible for the neuroprotective effects. In the present study, we truncated OPNpt20 to 13 or

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3

Shayakhmetov, Dmitry M., Andrea M. Eberly, Zong-Yi Li, and André Lieber. "Deletion of Penton RGD Motifs Affects the Efficiency of both the Internalization and the Endosome Escape of Viral Particles Containing Adenovirus Serotype 5 or 35 Fiber Knobs." Journal of Virology 79, no. 2 (2005): 1053–61. http://dx.doi.org/10.1128/jvi.79.2.1053-1061.2005.

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ABSTRACT Adenovirus (Ad) vectors are widely used for gene delivery in vitro and in vivo. A solid understanding of the biology of this virus is imperative for the development of novel, effective, and safe vectors. For the group C adenovirus serotypes 2 and 5 that use CAR as a primary attachment receptor, it is known that the penton base RGD motifs interact with cellular integrins and that this interaction promotes virus internalization. However, the RGD motif's impact on the efficiency of postinternalization steps, such as the escape of the virus particle from the endosome, is less defined. Fur

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4

Stamm, Nils, Kristin Glotzbach, Andreas Faissner, and Ralf Weberskirch. "Concentration Dependent Effect of Quaternary Amines on the Adhesion of U251-MG Cells." Gels 8, no. 12 (2022): 827. http://dx.doi.org/10.3390/gels8120827.

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Cationic gels have seen increasing interest in recent years for 2D cell cultivation since they may represent an alternative to the well-known RGD-peptide motif functionalized gels. However, few hydrogel systems with adjustable cationic strength have been fabricated and investigated so far. In this work, eight gels with defined concentrations of cationic groups, two of which also contained the RGD peptide, were prepared from three well-defined, soluble precursor copolymers with thiol-functionalities and PEGDA3500 as a crosslinker via thiol-ene chemistry. Live/dead stainings of U-251-MG cells on

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5

Zimmermann, Liza, Ernst Peterhans, and Joachim Frey. "RGD Motif of Lipoprotein T, Involved in Adhesion of Mycoplasma conjunctivae to Lamb Synovial Tissue Cells." Journal of Bacteriology 192, no. 14 (2010): 3773–79. http://dx.doi.org/10.1128/jb.00253-10.

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ABSTRACT Lipoprotein T (LppT), a membrane-located 105-kDa lipoprotein of Mycoplasma conjunctivae, the etiological agent of infectious keratoconjunctivitis (IKC) of domestic sheep and wild Caprinae, was characterized. LppT was shown to promote cell attachment to LSM 192 primary lamb joint synovial cells. Adhesion of M. conjunctivae to LSM 192 cells is inhibited by antibodies directed against LppT. The RGD (Arg-Gly-Asp) motif of LppT was found to be a specific site for binding of M. conjunctivae to these eukaryotic host cells. Recombinant LppT fixed to polymethylmethacrylate slides binds LSM 192

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6

Boonyakiat, Yingmanee, Pamela J. Hughes, Farideh Ghazi, and Glyn Stanway. "Arginine-Glycine-Aspartic Acid Motif Is Critical for Human Parechovirus 1 Entry." Journal of Virology 75, no. 20 (2001): 10000–10004. http://dx.doi.org/10.1128/jvi.75.20.10000-10004.2001.

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ABSTRACT The human parechovirus 1 RGD motif in VP1 was studied by mutagenesis. An RGD-to-RGE change gave only revertant viruses with a restored RGD, while deletion of GD was lethal and nonrevertable. Mutations at the +1 and +2 positions had some effect on growth properties and a +1 M-to-P change was lethal. These studies indicate that the RGD motif plays a critical role in infectivity, presumably by interacting with integrins, and that downstream amino acids can have an influence on function.

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7

Bugatti, Antonella, Federica Filippini, Marta Bardelli та ін. "SARS-CoV-2 Infects Human ACE2-Negative Endothelial Cells through an αvβ3 Integrin-Mediated Endocytosis Even in the Presence of Vaccine-Elicited Neutralizing Antibodies". Viruses 14, № 4 (2022): 705. http://dx.doi.org/10.3390/v14040705.

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Integrins represent a gateway of entry for many viruses and the Arg-Gly-Asp (RGD) motif is the smallest sequence necessary for proteins to bind integrins. All Severe Acute Respiratory Syndrome Virus type 2 (SARS-CoV-2) lineages own an RGD motif (aa 403–405) in their receptor binding domain (RBD). We recently showed that SARS-CoV-2 gains access into primary human lung microvascular endothelial cells (HL-mECs) lacking Angiotensin-converting enzyme 2 (ACE2) expression through this conserved RGD motif. Following its entry, SARS-CoV-2 remodels cell phenotype and promotes angiogenesis in the absence

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8

Reyer, Anja, Nancy Schindler, Daniela Ohde, et al. "The RGD sequence present in IGFBP-2 is required for reduced glucose clearance after oral glucose administration in female transgenic mice." American Journal of Physiology-Endocrinology and Metabolism 309, no. 4 (2015): E409—E417. http://dx.doi.org/10.1152/ajpendo.00168.2015.

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Recent studies suggest that insulin-like growth factor-binding protein-2 (IGFBP-2) affects both growth and metabolism. Whereas negative growth effects are primarily due to negative interference with IGF-I, the mechanisms for metabolic interference of IGFBP-2 are less clear. As we demonstrate, overexpression of IGFBP-2 in transgenic mice is correlated with a decelerated clearance of blood glucose after oral administration. IGFBP-2 carries an integrin-binding domain (RGD motif), which has been shown to also mediate IGF-independent effects. We thus asked if higher serum levels of IGFBP-2 without

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Cavenague, Maria F., Aline F. Teixeira, Luis G. V. Fernandes, and Ana L. T. O. Nascimento. "LIC12254 Is a Leptospiral Protein That Interacts with Integrins via the RGD Motif." Tropical Medicine and Infectious Disease 8, no. 5 (2023): 249. http://dx.doi.org/10.3390/tropicalmed8050249.

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Pathogenic leptospires can bind to receptors on mammalian cells such as cadherins and integrins. Leptospira effectively adheres to cells, overcomes host barriers and spreads into the bloodstream, reaching internal target organs such as the lungs, liver and kidneys. Several microorganisms produce proteins that act as ligands of integrins through the RGD motif. Here, we characterized a leptospiral RGD-containing protein encoded by the gene lic12254. In silico analysis of pathogenic, intermediate and saprophytic species showed that LIC12254 is highly conserved among pathogenic species, and is uni

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10

Basani, Ramesh B., Hua Zhu, Michael A. Thornton та ін. "Species differences in small molecule binding to αIIbβ3 are the result of sequence differences in 2 loops of the αIIb β propeller". Blood 113, № 4 (2009): 902–10. http://dx.doi.org/10.1182/blood-2008-09-177337.

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Abstract Compared with human platelets, rodent platelets are less responsive to peptides and peptidomimetics containing an arginine-glycine-aspartic acid (RGD) motif. Using chimeric human-rat αIIbβ3 molecules, we found that this difference in Arg-Gly-Asp-Ser (RGDS) sensitivity was the result of amino acid substitutions at residues 157, 159, and 162 in the W3:4-1 loop and an Asp-His replacement at residue 232 in the W4:4-1 loop of the αIIb β propeller. Introducing the entire rat W3:4-1 and W4:4-1 loops into human αIIbβ3 also decreased the inhibitory effect of the disintegrins, echistatin and er

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11

Bi, Qun, Xue Zhou, Xiaodong Cen, et al. "Efficient targeted anticoagulant with active RGD motif." Thrombosis Research 120, no. 4 (2007): 541–47. http://dx.doi.org/10.1016/j.thromres.2006.11.013.

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12

Vallon, Mario, Philipp Aubele, Klaus-Peter Janssen, and Markus Essler. "Thrombin-induced shedding of tumour endothelial marker 5 and exposure of its RGD motif are regulated by cell-surface protein disulfide-isomerase." Biochemical Journal 441, no. 3 (2012): 937–44. http://dx.doi.org/10.1042/bj20111682.

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TEM5 (tumour endothelial marker 5; also known as GPR124) is an adhesion G-protein-coupled receptor containing a cryptic RGD motif in its extracellular domain. TEM5 is expressed in endothelial cells and pericytes during angiogenesis. In the present paper, we report that thrombin mediates shedding of an N-terminal TEM5 fragment of 60 kDa (termed N60) containing the RGD motif in an open conformation. Thrombin directly cleaved rsTEM5 (recombinant soluble TEM5) 5 and 34 residues downstream of the RGD motif, resulting in formation of N60 and its C-terminal counterpart (termed C50). Interestingly, N6

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13

Kang, Zhao, Yining Wang, Jingjing Xu, et al. "An RGD-Containing Peptide Derived from Wild Silkworm Silk Fibroin Promotes Cell Adhesion and Spreading." Polymers 10, no. 11 (2018): 1193. http://dx.doi.org/10.3390/polym10111193.

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Arginine-Glycine-Aspartate (RGD) tripeptide can promote cell adhesion when present in the amino acid of proteins such as fibronectin. In order to demonstrate the bioactivity of an RGD-containing silk protein, a gene encoding the RGD motif-containing peptide GSGAGGRGDGGYGSGSS (–RGD–) derived from nonmulberry silk was designed and cloned, then multimerised and inserted into a commercial pGEX expression vector for recombinant expression of (–RGD–)n peptides. Herein, we focus on two glutathione-S-transferase (GST)-tagged fusion proteins, GST–(–RGD–)4 and GST–(–RGD–)8, which were expressed in Esche

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14

Liu, Yijuan, Lina Fan, Xuemei Lin, et al. "Functionalized self-assembled peptide RAD/Dentonin hydrogel scaffold promotes dental pulp regeneration." Biomedical Materials 17, no. 1 (2021): 015009. http://dx.doi.org/10.1088/1748-605x/ac3928.

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Abstract RADA16-I is an ion-complementary self-assembled peptide with a regular folded secondary conformation and can be assembled into an ordered nanostructure. Dentonin is an extracellular matrix phosphate glycoprotein functional peptide motif-containing RGD and SGDG motifs. In this experiment, we propose to combine RAD and Dentonin to form a functionalized self-assembled peptide RAD/Dentonin hydrogel scaffold. Furthermore, we expect that the RAD with the addition of functional motif Dentonin can promote pulp regeneration. The study analyzed the physicochemical properties of RAD/Dentonin thr

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15

Takahashi, Seiichiro, Michael Leiss, Markus Moser, et al. "The RGD motif in fibronectin is essential for development but dispensable for fibril assembly." Journal of Cell Biology 178, no. 1 (2007): 167–78. http://dx.doi.org/10.1083/jcb.200703021.

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Fibronectin (FN) is secreted as a disulfide-bonded FN dimer. Each subunit contains three types of repeating modules: FN-I, FN-II, and FN-III. The interactions of α5β1 or αv integrins with the RGD motif of FN-III repeat 10 (FN-III10) are considered an essential step in the assembly of FN fibrils. To test this hypothesis in vivo, we replaced the RGD motif with the inactive RGE in mice. FN-RGE homozygous embryos die at embryonic day 10 with shortened posterior trunk, absent tail bud–derived somites, and severe vascular defects resembling the phenotype of α5 integrin–deficient mice. Surprisingly,

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16

Springer, Timothy A., Jianghai Zhu та Tsan Xiao. "Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3". Journal of Cell Biology 182, № 4 (2008): 791–800. http://dx.doi.org/10.1083/jcb.200801146.

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Hemostasis and thrombosis (blood clotting) involve fibrinogen binding to integrin αIIbβ3 on platelets, resulting in platelet aggregation. αvβ3 binds fibrinogen via an Arg-Asp-Gly (RGD) motif in fibrinogen's α subunit. αIIbβ3 also binds to fibrinogen; however, it does so via an unstructured RGD-lacking C-terminal region of the γ subunit (γC peptide). These distinct modes of fibrinogen binding enable αIIbβ3 and αvβ3 to function cooperatively in hemostasis. In this study, crystal structures reveal the integrin αIIbβ3–γC peptide interface, and, for comparison, integrin αIIbβ3 bound to a lamprey γC

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17

Liu, MM, WT Li, XM Xia, F. Wang, M. MacDougall, and S. Chen. "Dentine sialophosphoprotein signal in dentineogenesis and dentine regeneration." European Cells and Materials 42 (July 18, 2021): 43–62. http://dx.doi.org/10.22203/ecm.v042a04.

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Dentineogenesis starts on odontoblasts, which synthesise and secrete non-collagenous proteins (NCPs) and collagen. When dentine is injured, dental pulp progenitors/mesenchymal stem cells (MSCs) can migrate to the injured area, differentiate into odontoblasts and facilitate formation of reactionary dentine. Dental pulp progenitor cell/MSC differentiation is controlled at given niches. Among dental NCPs, dentine sialophosphoprotein (DSPP) is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family, whose members share common biochemical characteristics such as an Arg-

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18

Healy, Judith M., Mitsuru Haruki, and Masakazu Kikuchi. "Preferred Motif for Integrin Binding Identified Using a Library of Randomized RGD Peptides Displayed on Phage." Protein & Peptide Letters 3, no. 1 (1996): 23–30. http://dx.doi.org/10.2174/092986650301220608153153.

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Abstract: We have selected RGD peptides recognized efficiently by integrin av3 through randomization of amino acids flanking the RGD motif. Degenerate RGD peptides were displayed on phage as fusions to the N-terminus of major coat protein Vill of M13 using a specially constructed phagemid vector. Identification of an apparent consensus sequence among ligands preferred by av3 supports the view that amino acids in the vicinity of RGD can influence receptor recognition of phage-peptides. In addition, several phage isolates encoded a potentially cyclic peptide which bound to av3 with superior affi

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19

Tan, Boon-Huan, Emma Nason, Norbert Staeuber, Wenrong Jiang, Katherine Monastryrskaya, and Polly Roy. "RGD Tripeptide of Bluetongue Virus VP7 Protein Is Responsible for Core Attachment to Culicoides Cells." Journal of Virology 75, no. 8 (2001): 3937–47. http://dx.doi.org/10.1128/jvi.75.8.3937-3947.2001.

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ABSTRACT Bluetongue virus (BTV) is an arthropod-borne virus transmitted byCulicoides species to vertebrate hosts. The double-capsid virion is infectious for Culicoides vector and mammalian cells, while the inner core is infectious for onlyCulicoides-derived cells. The recently determined crystal structure of the BTV core has revealed an accessible RGD motif between amino acids 168 to 170 of the outer core protein VP7, whose structure and position would be consistent with a role in cell entry. To delineate the biological role of the RGD sequence within VP7, we have introduced point mutations in

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20

MONLEÓN, Daniel, Vicent ESTEVE, Helena KOVACS, Juan J. CALVETE, and Bernardo CELDA. "Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR." Biochemical Journal 387, no. 1 (2005): 57–66. http://dx.doi.org/10.1042/bj20041343.

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Echistatin is a potent antagonist of the integrins αvβ3, α5β1 and αIIbβ3. Its full inhibitory activity depends on an RGD (Arg-Gly-Asp) motif expressed at the tip of the integrin-binding loop and on its C-terminal tail. Previous NMR structures of echistatin showed a poorly defined integrin-recognition sequence and an incomplete C-terminal tail, which left the molecular basis of the functional synergy between the RGD loop and the C-terminal region unresolved. We report a high-resolution structure of echistatin and an analysis of its internal motions by off-resonance ROESY (rotating-frame Overhau

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21

Manning, Viola A., Rachael M. Andrie, Aaron F. Trippe, and Lynda M. Ciuffetti. "Ptr ToxA Requires Multiple Motifs for Complete Activity." Molecular Plant-Microbe Interactions® 17, no. 5 (2004): 491–501. http://dx.doi.org/10.1094/mpmi.2004.17.5.491.

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Ptr ToxA was the first proteinaceous necrosis-inducing toxin identified and cloned from the wheat pathogen, Pyrenophora tritici-repentis. How this protein causes necrosis in sensitive wheat cultivars is not known. In an effort to understand the structural features of Ptr ToxA required for induction of necrosis, we employed a combination of site-directed mutagenesis and peptide inhibition studies. Mutagenesis was carried out on conserved motifs within the active domain of Ptr ToxA. Proteins with mutations of potential casein kinase 2 phosphorylation sites but not protein kinase C phosphorylatio

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22

Takagi, J. "Structural basis for ligand recognition by RGD (Arg-Gly-Asp)-dependent integrins." Biochemical Society Transactions 32, no. 3 (2004): 403–6. http://dx.doi.org/10.1042/bst0320403.

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Since the discovery of the RGD sequence motif as the essential cell attachment site in Fn (fibronectin), RGD-dependent ligand recognition by integrins has been the major focus of many integrin researches. Although many integrins recognize RGD-containing ligands, it is believed that residues outside the RGD motif provide specificity as well as high affinity for each integrin–ligand pair. These ‘secondary’ sites are generally assumed to interact directly with the α subunit of integrin, whereas the RGD motif binds primarily to the β subunit. This necessitates that the integrin–ligand interface co

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Williams, Çiğdem H., Tommi Kajander, Timo Hyypiä, Terry Jackson, Dean Sheppard та Glyn Stanway. "Integrin αvβ6 Is an RGD-Dependent Receptor for Coxsackievirus A9". Journal of Virology 78, № 13 (2004): 6967–73. http://dx.doi.org/10.1128/jvi.78.13.6967-6973.2004.

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ABSTRACT Coxsackievirus A9 (CAV9), a member of the Enterovirus genus of Picornaviridae, is a common human pathogen and is one of a significant number of viruses containing a functional arginine-glycine-aspartic acid (RGD) motif in one of their capsid proteins. Previous studies identified the RGD-recognizing integrin αvβ3 as its cellular receptor. However, integrin αvβ6 has been shown to be an efficient receptor for another RGD-containing picornavirus, foot-and-mouth disease virus (FMDV). In view of the similarity in sequence context of the RGD motifs in CAV9 and FMDV, we investigated whether α

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24

Waters, Christopher M., Carol L. Wells, and Gary M. Dunny. "The Aggregation Domain of Aggregation Substance, Not the RGD Motifs, Is Critical for Efficient Internalization by HT-29 Enterocytes." Infection and Immunity 71, no. 10 (2003): 5682–89. http://dx.doi.org/10.1128/iai.71.10.5682-5689.2003.

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ABSTRACT Aggregation substance (AS), a surface protein encoded on the pheromone-inducible plasmids of Enterococcus faecalis, has been shown to increase adherence and internalization into a number of different cell types, presumably through integrin binding mediated by the N-terminal RGD motif of AS. Here, defined mutations constructed in Asc10, the AS encoded by the plasmid pCF10, are analyzed for their ability to promote increased internalization levels into HT-29 enterocytes. The results clearly show that the previously identified Asc10 functional domain, not the RGD motifs, is critical for

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Süßmuth, Sigurd D., Albrecht Muscholl-Silberhorn, Reinhard Wirth, Milorad Susa, Reinhard Marre, and Eva Rozdzinski. "Aggregation Substance Promotes Adherence, Phagocytosis, and Intracellular Survival of Enterococcus faecalis within Human Macrophages and Suppresses Respiratory Burst." Infection and Immunity 68, no. 9 (2000): 4900–4906. http://dx.doi.org/10.1128/iai.68.9.4900-4906.2000.

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ABSTRACT The aggregation substance (AS) of Enterococcus faecalis, encoded on sex pheromone plasmids, is a surface-bound glycoprotein that mediates aggregation between bacteria thereby facilitating plasmid transfer. Sequencing of the pAD1-encoded Asa1 revealed that this surface protein contains two RGD motifs which are known to ligate integrins. Therefore, we investigated the influence of AS on the interaction of E. faecalis with human monocyte-derived macrophages which constitutively express β2 integrins (e.g., CD18). AS was found to cause a greater-than-fivefold increase in enterococcal adher

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26

Bailey, Kate, Volkan Çevik, Nicholas Holton, et al. "Molecular Cloning of ATR5Emoy2 from Hyaloperonospora arabidopsidis, an Avirulence Determinant That Triggers RPP5-Mediated Defense in Arabidopsis." Molecular Plant-Microbe Interactions® 24, no. 7 (2011): 827–38. http://dx.doi.org/10.1094/mpmi-12-10-0278.

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RPP5 is the seminal example of a cytoplasmic NB-LRR receptor-like protein that confers downy mildew resistance in Arabidopsis thaliana. In this study, we describe the cloning and molecular characterization of the gene encoding ATR5Emoy2, an avirulence protein from the downy mildew pathogen Hyaloperonospora arabidopsidis isolate Emoy2. ATR5Emoy2 triggers defense response in host lines expressing the functional RPP5 allele from Landsberg erecta (Ler-0). ATR5Emoy2 is embedded in a cluster with two additional ATR5-like (ATR5L) genes, most likely resulting from gene duplications. ATR5L proteins do

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27

D'Souza, Stanley E., Mark H. Ginsberg, and Edward F. Plow. "Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif." Trends in Biochemical Sciences 16 (January 1991): 246–50. http://dx.doi.org/10.1016/0968-0004(91)90096-e.

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Baranowski, Eric, Carmen M. Ruiz-Jarabo, Noemi Sevilla, David Andreu, Ewald Beck, and Esteban Domingo. "Cell Recognition by Foot-and-Mouth Disease Virus That Lacks the RGD Integrin-Binding Motif: Flexibility in Aphthovirus Receptor Usage." Journal of Virology 74, no. 4 (2000): 1641–47. http://dx.doi.org/10.1128/jvi.74.4.1641-1647.2000.

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ABSTRACT Cell surface molecules that can act as virus receptors may exert an important selective pressure on RNA viral quasispecies. Large population passages of foot-and-mouth disease virus (FMDV) in cell culture select for mutant viruses that render dispensable a highly conserved Arg-Gly-Asp (RGD) motif responsible for integrin receptor recognition. Here, we provide evidence that viability of recombinant FMDVs including a Asp-143→Gly change at the RGD motif was conditioned by a number of capsid substitutions selected upon FMDV evolution in cell culture. Multiply passaged FMDVs acquired the a

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Madisch, Ijad, Soeren Hofmayer, Christian Moritz, et al. "Phylogenetic Analysis and Structural Predictions of Human Adenovirus Penton Proteins as a Basis for Tissue-Specific Adenovirus Vector Design." Journal of Virology 81, no. 15 (2007): 8270–81. http://dx.doi.org/10.1128/jvi.00048-07.

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ABSTRACT The penton base is a major capsid protein of human adenoviruses (HAdV) which forms the vertices of the capsid and interacts with hexon and fiber protein. Two hypervariable loops of the penton are exposed on the capsid surface. Sequences of these and 300 adjacent amino acid residues of all 51 HAdV and closely related simian adenoviruses were studied. Adjacent sequences and predicted overall secondary structure were conserved. Phylogenetic analysis revealed clustering corresponding to the HAdV species and recombination events in the origin of HAdV prototypes. All HAdV except serotypes 4

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HELLWAGE, Jens, Sabine KÜHN, and Peter F. ZIPFEL. "The human complement regulatory factor-H-like protein 1, which represents a truncated form of factor H, displays cell-attachment activity." Biochemical Journal 326, no. 2 (1997): 321–27. http://dx.doi.org/10.1042/bj3260321.

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Complement factor H (FH) and factor-H-like protein 1 (FHL-1) are human plasma proteins with regulatory functions in the alternative pathway of complement activation. FH and FHL-1 are organized in repetitive elements termed short consensus repeats (SCRs) and the seven SCRs of FHL-1 are identical with the N-terminal domain of the 20 SCRs of FH. The fourth SCR of both proteins (SCR 4) includes the sequence Arg-Gly-Asp (RGD), a motif that is responsible for the major adhesive activity of matrix proteins like fibronectin. A synthetic hexapeptide with the sequence ERGDAV derived from the RGD domain

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LUDBROOK, Steven B., Simon T. BARRY, Chris J. DELVES, and Carmel M. T. HORGAN. "The integrin alphavbeta3 is a receptor for the latency-associated peptides of transforming growth factors beta1 and beta3." Biochemical Journal 369, no. 2 (2003): 311–18. http://dx.doi.org/10.1042/bj20020809.

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The integrins αvβ1, αvβ5, αvβ6 and αvβ8 have all recently been shown to interact with the RGD motif of the latency-associated peptide (LAPβ1) of transforming growth factor β1 (TGFβ1), with binding to αvβ6 and αvβ8 leading to TGFβ1 activation. Previously it has been suggested that the remaining αv integrin, αvβ3, does not interact with LAPβ1. However, here we show clearly that αvβ3 does indeed interact with the LAPβ1 RGD motif. This interaction is similar to other αvβ3 ligands in terms of the cations required for adhesion, the concentrations of LAPβ1 required for binding and the ability of a sm

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Koizumi, Naoya, Hiroyuki Mizuguchi, Fuminori Sakurai, Teruhide Yamaguchi, Yoshiteru Watanabe та Takao Hayakawa. "Reduction of Natural Adenovirus Tropism to Mouse Liverby Fiber-Shaft Exchange in Combination with both CAR- andαv Integrin-BindingAblation". Journal of Virology 77, № 24 (2003): 13062–72. http://dx.doi.org/10.1128/jvi.77.24.13062-13072.2003.

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ABSTRACT The primary receptor, the coxsackievirus and adenovirus receptor (CAR), and the secondary receptor, αv integrins, are the tropism determinants of adenovirus (Ad) type 5. Inhibition of the interaction of both the fiber with CAR and the penton base with the αv integrin appears to be crucial to the development of targeted Ad vectors, which specifically transduce a given cell population. In this study, we developed Ad vectors with ablation of both CAR and αv integrin binding by mutating the fiber knob and the RGD motif of the penton base. We also replaced the fiber shaft domain with that

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Logunov, Denis Y., Olga V. Zubkova, Anna S. Karyagina-Zhulina, et al. "Identification of HI-Like Loop in CELO Adenovirus Fiber for Incorporation of Receptor Binding Motifs." Journal of Virology 81, no. 18 (2007): 9641–52. http://dx.doi.org/10.1128/jvi.00534-07.

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ABSTRACT Vectors based on the chicken embryo lethal orphan (CELO) avian adenovirus (Ad) have two attractive properties for gene transfer applications: resistance to preformed immune responses to human Ads and the ability to grow in chicken embryos, allowing low-cost production of recombinant viruses. However, a major limitation of this technology is that CELO vectors demonstrate decreased efficiency of gene transfer into cells expressing low levels of the coxsackie-Ad receptor (CAR). In order to improve the efficacy of gene transfer into CAR-deficient cells, we modified viral tropism via genet

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Li, Na, Simei Qiu, Ying Fang, Jianhua Wu та Quhuan Li. "Comparison of Linear vs. Cyclic RGD Pentapeptide Interactions with Integrin αvβ3 by Molecular Dynamics Simulations". Biology 10, № 7 (2021): 688. http://dx.doi.org/10.3390/biology10070688.

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Integrin αvβ3 interacting with the short Arg-Gly-Asp (RGD) motif plays a critical role in the progression of several types of tumors. However, the effects of the RGD structure (cyclic or linear) with integrin αvβ3 at the atomic level remain poorly understood. Here, we performed association and dissociation dynamic simulations for integrin αvβ3 in complex with a linear or cyclic pentapeptide by steered molecular dynamics simulations. Compared with cyclic RGD, the linear RGD peptide triggers instability of the configurational changes, mainly resting with the RGD domain due to its flexibility. Th

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Magnusson, Maria K., Saw See Hong, Pierre Boulanger, and Leif Lindholm. "Genetic Retargeting of Adenovirus: Novel Strategy Employing “Deknobbing” of the Fiber." Journal of Virology 75, no. 16 (2001): 7280–89. http://dx.doi.org/10.1128/jvi.75.16.7280-7289.2001.

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ABSTRACT For efficient and versatile use of adenovirus (Ad) as an in vivo gene therapy vector, modulation of the viral tropism is highly desirable. In this study, a novel method to genetically alter the Ad fiber tropism is described. The knob and the last 15 shaft repeats of the fiber gene were deleted and replaced with an external trimerization motif and a new cell-binding ligand, in this case the integrin-binding motif RGD. The corresponding recombinant fiber retained the basic biological functions of the natural fiber, i.e., trimerization, nuclear import, penton formation, and ligand bindin

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Tsai, Wan-Hua, Chia-Wen Chang, Yee-Shin Lin та ін. "Streptococcal Pyrogenic Exotoxin B-Induced Apoptosis in A549 Cells Is Mediated through αvβ3 Integrin and Fas". Infection and Immunity 76, № 4 (2008): 1349–57. http://dx.doi.org/10.1128/iai.01162-07.

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ABSTRACT Our previous work suggested that streptococcal pyrogenic exotoxin (SPE) B-induced apoptosis is mediated through a receptor-like mechanism. In this study, we have identified αvβ3 and Fas as the SPE B receptors for this function. The SPE B fragment without the RGD motif and G308S, a SPE B mutant with the RSD motif, induced less apoptosis than did native SPE B, suggesting that the RGD motif is critical for SPE B-induced apoptosis. Fluorescein isothiocyanate-SPE B binding assays and immunoprecipitation analysis showed that SPE B specifically interacted with αvβ3. Anti-αvβ3 antibody partia

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DUBLJEVIC, Valentina, Adnan SALI, and James W. GODING. "A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin." Biochemical Journal 341, no. 1 (1999): 11–14. http://dx.doi.org/10.1042/bj3410011.

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The transferrin receptor contains a highly conserved Arg-Gly-Asp (RGD) sequence in the C-terminal region where transferrin is thought to bind. RGD sequences are commonly involved in cell adhesion. This sequence is crucial for transferrin binding, suggesting possible evolutionary links between molecules mediating iron uptake and cell adhesion.

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Nader, Danielle, and Steve W. Kerrigan. "Molecular Cross-Talk between Integrins and Cadherins Leads to a Loss of Vascular Barrier Integrity during SARS-CoV-2 Infection." Viruses 14, no. 5 (2022): 891. http://dx.doi.org/10.3390/v14050891.

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The vascular barrier is heavily injured following SARS-CoV-2 infection and contributes enormously to life-threatening complications in COVID-19. This endothelial dysfunction is associated with the phlogistic phenomenon of cytokine storms, thrombotic complications, abnormal coagulation, hypoxemia, and multiple organ failure. The mechanisms surrounding COVID-19 associated endotheliitis have been widely attributed to ACE2-mediated pathways. However, integrins are emerging as possible receptor candidates for SARS-CoV-2, and their complex intracellular signaling events are essential for maintaining

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Nader, Danielle, and Steve W. Kerrigan. "Molecular Cross-Talk between Integrins and Cadherins Leads to a Loss of Vascular Barrier Integrity during SARS-CoV-2 Infection." Viruses 14, no. 5 (2022): 891. http://dx.doi.org/10.3390/v14050891.

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The vascular barrier is heavily injured following SARS-CoV-2 infection and contributes enormously to life-threatening complications in COVID-19. This endothelial dysfunction is associated with the phlogistic phenomenon of cytokine storms, thrombotic complications, abnormal coagulation, hypoxemia, and multiple organ failure. The mechanisms surrounding COVID-19 associated endotheliitis have been widely attributed to ACE2-mediated pathways. However, integrins are emerging as possible receptor candidates for SARS-CoV-2, and their complex intracellular signaling events are essential for maintaining

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Nader, Danielle, and Steve W. Kerrigan. "Molecular Cross-Talk between Integrins and Cadherins Leads to a Loss of Vascular Barrier Integrity during SARS-CoV-2 Infection." Viruses 14, no. 5 (2022): 891. http://dx.doi.org/10.3390/v14050891.

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The vascular barrier is heavily injured following SARS-CoV-2 infection and contributes enormously to life-threatening complications in COVID-19. This endothelial dysfunction is associated with the phlogistic phenomenon of cytokine storms, thrombotic complications, abnormal coagulation, hypoxemia, and multiple organ failure. The mechanisms surrounding COVID-19 associated endotheliitis have been widely attributed to ACE2-mediated pathways. However, integrins are emerging as possible receptor candidates for SARS-CoV-2, and their complex intracellular signaling events are essential for maintaining

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Casal, J. Ignacio, and Rubén A. Bartolomé. "Beyond N-Cadherin, Relevance of Cadherins 5, 6 and 17 in Cancer Progression and Metastasis." International Journal of Molecular Sciences 20, no. 13 (2019): 3373. http://dx.doi.org/10.3390/ijms20133373.

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Cell-cell adhesion molecules (cadherins) and cell-extracellular matrix adhesion proteins (integrins) play a critical role in the regulation of cancer invasion and metastasis. Although significant progress has been made in the characterization of multiple members of the cadherin superfamily, most of the published work continues to focus in the switch E-/N-cadherin and its role in the epithelial–mesenchymal transition. Here, we will discuss the structural and functional properties of a subset of cadherins (cadherin 17, cadherin 5 and cadherin 6) that have an RGD motif in the extracellular domain

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Garrigues, H. Jacques, Yelena E. Rubinchikova, C. Michael DiPersio та Timothy M. Rose. "Integrin αVβ3 Binds to the RGD Motif of Glycoprotein B of Kaposi's Sarcoma-Associated Herpesvirus and Functions as an RGD-Dependent Entry Receptor". Journal of Virology 82, № 3 (2007): 1570–80. http://dx.doi.org/10.1128/jvi.01673-07.

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ABSTRACT Kaposi's sarcoma-associated herpesvirus (KSHV) envelope-associated glycoprotein B (gB) is involved in the initial steps of binding to host cells during KSHV infection. gB contains an RGD motif reported to bind the integrin α3β1 during virus entry. Although the ligand specificity of α3β1 has been controversial, current literature indicates that α3β1 ligand recognition is independent of RGD. We compared α3β1 to the RGD-binding integrin, αVβ3, for binding to envelope-associated gB and a gB(RGD) peptide. Adhesion assays demonstrated that β3-CHO cells overexpressing αVβ3 specifically bound

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Wang, Fu-Zhang, Shaw M. Akula, Neelam Sharma-Walia, Ling Zeng, and Bala Chandran. "Human Herpesvirus 8 Envelope Glycoprotein B Mediates Cell Adhesion via Its RGD Sequence." Journal of Virology 77, no. 5 (2003): 3131–47. http://dx.doi.org/10.1128/jvi.77.5.3131-3147.2003.

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ABSTRACT Human herpesvirus 8 (HHV-8) or Kaposi's sarcoma-associated herpesvirus, implicated in the pathogenesis of Kaposi's sarcoma, utilizes heparan sulfate-like molecules to bind the target cells via its envelope-associated glycoproteins gB and gpK8.1A. HHV-8-gB possesses the Arg-Gly-Asp (RGD) motif, the minimal peptide region of many proteins known to interact with subsets of host cell surface integrins. HHV-8 utilizes α3β1 integrin as one of the receptors for its entry into the target cells via its gB interaction and induces the activation of focal adhesion kinase (FAK) (S. M. Akula, N. P.

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Wheaton, Amanda K., Miranda Velikoff, Manisha Agarwal та ін. "The vitronectin RGD motif regulates TGF-β-induced alveolar epithelial cell apoptosis". American Journal of Physiology-Lung Cellular and Molecular Physiology 310, № 11 (2016): L1206—L1217. http://dx.doi.org/10.1152/ajplung.00424.2015.

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Transforming growth factor-β (TGF-β) is a critical driver of acute lung injury and fibrosis. Injury leads to activation of TGF-β, which regulates changes in the cellular and matrix makeup of the lung during the repair and fibrosis phase. TGF-β can also initiate alveolar epithelial cell (AEC) apoptosis. Injury leads to destruction of the laminin-rich basement membrane, which is replaced by a provisional matrix composed of arginine-glycine-aspartate (RGD) motif-containing plasma matrix proteins, including vitronectin and fibronectin. To determine the role of specific matrix proteins on TGF-β-ind

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Hughes, P. J., C. Horsnell, T. Hyypiä, and G. Stanway. "The coxsackievirus A9 RGD motif is not essential for virus viability." Journal of virology 69, no. 12 (1995): 8035–40. http://dx.doi.org/10.1128/jvi.69.12.8035-8040.1995.

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Tamma, Grazia, Domenica Lasorsa, Marianna Ranieri, Lisa Mastrofrancesco, Giovanna Valenti, and Maria Svelto. "Integrin Signaling Modulates AQP2 Trafficking via Arg-Gly-Asp (RGD) Motif." Cellular Physiology and Biochemistry 27, no. 6 (2011): 739–48. http://dx.doi.org/10.1159/000330082.

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Wang, Jianjun, Yanping Cao, and Guojun Zheng. "Mutation in the RGD motif decreases the esterase activity of Xcc_est." Biotechnology Letters 31, no. 9 (2009): 1445–49. http://dx.doi.org/10.1007/s10529-009-0013-6.

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Nelsen-Salz, Birgit, Hans J. Eggers та Holger Zimmermann. "Integrin αvβ3 (vitronectin receptor) is a candidate receptor for the virulent echovirus 9 strain Barty". Journal of General Virology 80, № 9 (1999): 2311–13. http://dx.doi.org/10.1099/0022-1317-80-9-2311.

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The enterovirus echovirus 9 strain Barty (E9/Barty) is pathogenic for newborn mice as well as for humans. In contrast to the apathogenic prototype strain Hill, strain Barty encodes an RGD motif in the C-terminal part of the structural protein VP1. Data are presented that show that E9/Barty binds its target cells via contact of the RGD motif to the αvβ3 integrin (vitronectin receptor), whereas prototype Hill uses a different, still unidentified receptor site. Furthermore, virus titres of murine muscle tissue were compared after infection of newborn and 1-, 2-, 3- and 12-week-old mice. The repli

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Parry, Christopher, Susanne Bell, Tony Minson та Helena Browne. "Herpes simplex virus type 1 glycoprotein H binds to αvβ3 integrins". Journal of General Virology 86, № 1 (2005): 7–10. http://dx.doi.org/10.1099/vir.0.80567-0.

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Glycoprotein H (gH) homologues are found in all members of the herpes virus family, and gH is one of the virion envelope glycoproteins that is essential for virus entry. In this study, a recombinant soluble form of Herpes simplex virus type 1 (HSV-1) gH, in which the ectodomain is fused to the Fc-binding region of IgG, has been generated. This was expressed in mammalian cells together with gL and the resulting gHFc–gL heterodimer was purified using Protein A Sepharose. Low-affinity cell binding assays showed that gHFc–gL bound specifically to Vero cells and mutation of a potential integrin-bin

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Li, Li, Shumei Lin, and Feng Yang. "Characterization of an envelope protein (VP110) of White spot syndrome virus." Journal of General Virology 87, no. 7 (2006): 1909–15. http://dx.doi.org/10.1099/vir.0.81730-0.

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A protein of 110 kDa (termed VP110) from the envelope fraction of White spot syndrome virus (WSSV) was identified by SDS-PAGE and mass spectrometry. The resulting amino acid sequence matched an open reading frame (wsv035) containing an Arg–Gly–Asp (RGD) motif in the WSSV genome database. To validate the mass-spectrometry result, the C-terminal segment of the wsv035 open reading frame was expressed in Escherichia coli as a fusion protein, which was used to produce specific antibody. Analysis by Western blotting and immunoelectron microscopy demonstrated that VP110 was an envelope protein of WSS

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