INTERFERON SEQUENCE HOMOLOGY AND RECEPTOR BINDING ACTIVITY OF OVINE TROPHOBLAST ANTILUTEOLYTIC PROTEIN

1987 ◽  
Vol 115 (2) ◽  
pp. R13-R15 ◽  
Author(s):  
H.J. Stewart ◽  
S.H.E. McCann ◽  
P.J. Barker ◽  
K.E. Lee ◽  
G.E. Lamming ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Receptor Binding ◽  
Early Pregnancy ◽  
Sequence Homology ◽  
Binding Activity ◽  
Membrane Receptors ◽  
Interferon Α ◽  
Receptor Binding Activity ◽  
Terminal Amino

ABSTRACT Sequencing of the 40 N-terminal amino acids of the blastocyst protein responsible for blocking corpus luteum regression in early pregnancy in sheep revealed a 37% homology with human α-interferon; 28% of the remaining amino acid changes were conservative. 125I-Labelled human α-interferon bound to membrane receptors from sheep uteri with an approximate Kd of 4 × 10−11 M; binding was inhibited by unlabelled α-interferon or purified blastocyst antiluteolytic protein. The blastocyst antiluteolytic protein therefore closely resembles the interferon-α family of antiviral proteins.

Amino acids and peptides. LVI. Synthesis of pyrazinone ring-containing opioid mimetics and examination of their opioid receptor binding activity

Tetrahedron ◽  
1999 ◽  
Vol 55 (50) ◽  
pp. 14391-14406 ◽  
Author(s):  
Yoshio Okada ◽  
Atsuko Fukumizu ◽  
Motohiro Takahashi ◽  
Junpei Yamazaki ◽  
Toshio Yokoi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Opioid Receptor ◽  
Receptor Binding ◽  
Binding Activity ◽  
Receptor Binding Activity ◽  
Opioid Receptor Binding

scholarly journals The C Terminus of Component C2II ofClostridium botulinum C2 Toxin Is Essential for Receptor Binding

2000 ◽  
Vol 68 (8) ◽  
pp. 4566-4573 ◽  
Author(s):  
Dagmar Blöcker ◽  
Holger Barth ◽  
Elke Maier ◽  
Roland Benz ◽  
Joseph T. Barbieri ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Receptor Binding ◽  
Sodium Dodecyl ◽  
Cytotoxic Action ◽  
Amino Acid Residues ◽  
C Terminus ◽  
Terminal Amino ◽  
Function Relationship ◽  
C2 Toxin

ABSTRACT The binary Clostridium botulinum C2 toxin consists of two separate proteins, the binding component C2II (80.5 kDa) and the actin-ADP-ribosylating enzyme component C2I (49.4 kDa). For its cytotoxic action, C2II binds to a cell membrane receptor and induces cell entry of C2I via receptor-mediated endocytosis. Here we studied the structure-function relationship of C2II by constructing truncated C2II proteins and producing polyclonal antisera against selective regions of C2II. An antibody raised against the C terminus (amino acids 592 to 721) of C2II inhibited binding of C2II to cells. The antibody prevented pore formation by C2II oligomers in artificial membranes but did not influence the properties of existing channels. To further define the region responsible for receptor binding, we constructed proteins with deletions in C2II; specifically, they lacked amino acid residues 592 to 721 and the 7 C-terminal amino acid residues. The truncated proteins still formed sodium dodecyl sulfate-stable oligomers but were unable to bind to cells. Our data indicate that the C terminus of C2II mediates binding of the protein to cells and that the 7 C-terminal amino acids are structurally important for receptor binding.

ISOLATION AND CHARACTERIZATION OF cDNA CLONES FOR THE PLATELET MEMBRANE GLYCOPROTEINS IIb and IIIa

1987 ◽  
Author(s):  
A E Butler-Zimrin ◽  
J S Bennett ◽  
M Poncz ◽  
E Schwartz ◽  
S Surrey ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Transmembrane Domain ◽  
Platelet Membrane ◽  
Membrane Receptors ◽  
Cdna Clones ◽  
Single Chain ◽  
Platelet Protein ◽  
Isolation And Characterization ◽  
Terminal Amino

The platelet membrane GPIIb/GPIIIa complex on activated platelets contains receptors for fibrinogen, von Willebrand factor, and fibronectin. GPIIb and GPIlia also appear to be members of a family of membrane receptors involved in cell-cell and cell-matrix interactions. To study the structure of GPIIb and GPIIIa, we have constructed an expression library in the vector lambda gtll using mRNA from the HEL cell line and screened it with polyclonal antibody against each platelet protein. HEL cells constitutively express proteins similar to platelet GPIIb and GPIIIa. A 3.2kb GPIIb cDNA clone was identified that encodes for all 1008 amino acids of GPIIb including the known N-terminal amino acids of the α Cand βsubunits. This confirms that GPIIb is synthesized as a single chain polypeptide that is cleaved into two disulfide-linked subunits posttranslation. Analysis of the amino acid sequence revealed a major C-terminal transmembrane domain in the βsubunit, two potential transmembrane domains near the N-terminus of the αsubunit, and four possible N-linked glycosylation sites. Approximately 30% amino acid identity was found between GPIIb and the available amino acid sequences for the larger chains of the fibronectin and vitronectin receptors. Initial sequence analysis of a 3.8kb cDNA for GPIIIa included the known N-terminal amino acids of the platelet protein. Northern blot analysis was performed using HEL cell total RNA. The GPIIb cDNA hybridized to a 4.1kb mRNA while the GPIIIa cDNA hybridized to a 5.8kb mRNA. This indicates that the two cDNAs do not cross-hybridize and suggests that GPIIb and GPIIIa are encoded by separate genes. The availability of these cDNA for GPIIb and GPIIIa will facilitate study of the structure and function of the proteins and will aid in clarifying their relationship to other adhesive protein receptors.

scholarly journals The carboxyl terminus in apolipoprotein E2 and the seven amino acid repeat in apolipoprotein E-Leiden: role in receptor-binding activity

1998 ◽  
Vol 39 (6) ◽  
pp. 1173-1180 ◽  
Author(s):  
Li-Ming Dong ◽  
Thomas L. Innerarity ◽  
Kay S. Arnold ◽  
Yvonne M. Newhouse ◽  
Karl H. Weisgraber
Keyword(s):  
Amino Acid ◽  
Apolipoprotein E ◽  
Receptor Binding ◽  
Binding Activity ◽  
Carboxyl Terminus ◽  
Amino Acid Repeat ◽  
Receptor Binding Activity

Synthetic analogs of the carboxyl-terminus of .beta.-thyrotropin: the importance of basic amino acids in receptor binding activity

Biochemistry ◽  
1992 ◽  
Vol 31 (41) ◽  
pp. 10094-10098 ◽  
Author(s):  
Matthew C. Leinung ◽  
Elizabeth R. Bergert ◽  
Daniel J. McCormick ◽  
John C. Morris
Keyword(s):  
Amino Acids ◽  
Receptor Binding ◽  
Binding Activity ◽  
Carboxyl Terminus ◽  
Synthetic Analogs ◽  
Basic Amino Acids ◽  
Receptor Binding Activity

scholarly journals Role of the amino acid mutations in the HA gene of H9N2 avian influenza virus under selective pressure in escape vaccine antibodies

2021 ◽  
Author(s):  
Rui Zhu ◽  
Shunshun Xu ◽  
Wangyangji Sun ◽  
Quan Li ◽  
Huoying Shi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Antigenic Variation ◽  
Binding Activity ◽  
H9n2 Virus ◽  
Viral Escape ◽  
Inactivated Vaccine ◽  
Receptor Binding Activity ◽  
Amino Acid Mutations

AbstractIt has been well-documented that some amino acid mutations in hemagglutinin (HA) of H9N2 avian influenza virus (H9N2 virus) alter the viral antigenicity, but little is reported about the role of antibody escape mutations in escape vaccine antibodies. In this study, we found that the evolution of F/98 strain in chicken embryos or chickens resulted in significant differences in immune escape, and identify the contribution of HA mutations to the antigenic variation and immune escape of H9N2 virus. Among amino acid mutations in the HA of the antigen variant viruses occurring in embryonated chicken eggs and/or chickens with or without the selection pressure of vaccine antibodies, the mutations, S145N, Q164L, A168T, A198V, M224K and Q234L, affect the antigen drift of H9N2 virus. Specially, the A198V mutation, located at the receptor-binding site on the head domain of HA, significantly contributed the antigenic variation of H9N2 virus. The mutation A198V or Q234L significantly improved the receptor binding activity, while S145N mutation decreased the receptor binding activity. Single S145N mutation could promote viral escape from polyclonal antibodies (pAbs) by preventing Ab binding physically, and single A198V mutation could promote viral escape from pAbs by enhancing the receptor binding activity. Additionally, either the mutation S145N or A198V did interfere with the immunogenicity of the inactivated vaccine, resulting in reduction of the protective efficiency of H9N2 inactivated vaccine, which contributed escape from the antibody-based immunity. Our findings provided an important reference for the accurate evaluation of the role of the amino acids mutation in HA affecting the antigenicity of H9N2 virus on immune escape, and delivered a new perspective for monitoring the adaptive evolution of H9N2 virus.ImportanceIn this study, the role of the HA mutations of H9N2 virus occurring with and without antibody selective pressure on escaping from the antibody-based immune response in host was analyzed. The results demonstrated that (i) the HA mutations S145N, Q164L, A168T, A198V, M224K, and Q234L occurring in the process of the adaptive evolution of H9N2 virus in embryonated chicken eggs and/or chickens could affect the antigenic variation of H9N2 virus. Among these mutations, the HA mutation A198V had the most significant effect on the antigenic variation; (ii) S145N mutation promoted viral escape from pAbs by preventing Abs binding physically; (iii) A198V mutation did promote viral escape from pAbs by enhancing the receptor binding activity; (iv) neither the HA mutation S145N or A198V interfered with the immunogenicity of the inactivated vaccine, resulting in reduction of the protective efficiency of H9N2 inactivated vaccine.

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