scholarly journals The characterization of protein 4.1 Presles, a shortened variant of RBC membrane protein 4.1

Blood ◽  
1985 ◽  
Vol 65 (6) ◽  
pp. 1511-1517 ◽  
Author(s):  
L Morle ◽  
M Garbarz ◽  
N Alloisio ◽  
R Girot ◽  
I Chaveroche ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Membrane Protein ◽  
Limited Proteolysis ◽  
Genetic Data ◽  
Compound Heterozygote ◽  
Heterozygous State ◽  
Protein 4.1 ◽  
Rbc Membrane ◽  
The Family

Abstract In a previous report (Blood 60:265, 1982), we described a family with an abnormal RBC membrane protein doublet, which we considered a shortened protein 4.1 on the basis of biochemical and genetic data. Using an anti-4.1 monoclonal antibody, we confirm here that the shortened protein derives from protein 4.1. One of the members of the family contemporaneously displayed the 4.1 (-) trait, eg, the heterozygous state of this variety of hereditary elliptocytosis that lacks protein 4.1. The 4.1a/4.1b ratio was low whenever the 4.1 trait was present, regardless of the type of protein 4.1 involved. The RBCs of the compound heterozygote, containing only the shortened species of protein 4.1, made it possible to analyze without interference the contact between shortened protein 4.1 and sialoglycoprotein beta, or glycoconnectin. Shortened protein 4.1 did not alter the amount of glycoconnectin in the ghosts nor did it change its extractability into the Triton shells. Limited proteolysis of shortened polypeptides 4.1a and 4.1b showed that they are sequence related. It is conflicting that the persons carrying the shortened protein 4.1 are devoid of specific clinical and morphological abnormalities, apart from those pertaining to the 4.1- trait, when the latter is present.

scholarly journals Characterization of a Broadly Reactive Monoclonal Antibody against Norovirus Genogroups I and II: Recognition of a Novel Conformational Epitope

2007 ◽  
Vol 81 (22) ◽  
pp. 12298-12306 ◽  
Author(s):  
Tomoyuki Shiota ◽  
Michio Okame ◽  
Sayaka Takanashi ◽  
Pattara Khamrin ◽  
Makiko Takagi ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Conformational Epitope ◽  
The Novel ◽  
Antigen Specificity ◽  
Virus Like Particle ◽  
The Family ◽  
Immunological Diagnosis ◽  
Further Development

ABSTRACT Norovirus, which belongs to the family Caliciviridae, is one of the major causes of nonbacterial acute gastroenteritis in the world. The main human noroviruses are of genogroup I (GI) and genogroup II (GII), which were subdivided further into at least 15 and 18 genotypes (GI/1 to GI/15 and GII/1 to GII/18), respectively. The development of immunological diagnosis for norovirus had been hindered by the antigen specificity of the polyclonal antibody. Therefore, several laboratories have produced broadly reactive monoclonal antibodies, which recognize the linear GI and GII cross-reactive epitopes or the conformational GI-specific epitope. In this study, we characterized the novel monoclonal antibody 14-1 (MAb14-1) for further development of the rapid immunochromatography test. Our results demonstrated that MAb14-1 could recognize 15 recombinant virus-like particles (GI/1, 4, 8, and 11 and GII/1 to 7 and 12 to 15) and showed weak affinity to the virus-like particle of GI/3. This recognition range is the broadest of the existing monoclonal antibodies. The epitope for MAb14-1 was identified by fragment, sequence, structural, and mutational analyses. Both terminal antigenic regions (amino acid positions 418 to 426 and 526 to 534) on the C-terminal P1 domain formed the conformational epitope and were in the proximity of the insertion region (positions 427 to 525). These regions contained six amino acids responsible for antigenicity that were conserved among genogroup(s), genus, and Caliciviridae. This epitope mapping explained the broad reactivity and different titers among GI and GII. To our knowledge, we are the first group to identify the GI and GII cross-reactive monoclonal antibody, which recognizes the novel conformational epitope. From these data, MAb14-1 could be used further to develop immunochromatography.

scholarly journals Further characterization of erythrocyte p80 and the membrane protein defect of In(Lu) Lu(a-b-) erythrocytes

Blood ◽  
1987 ◽  
Vol 70 (5) ◽  
pp. 1475-1481
Author(s):  
MJ Telen ◽  
I Rogers ◽  
M Letarte
Keyword(s):  
Monoclonal Antibody ◽  
Membrane Protein ◽  
Concanavalin A ◽  
Polyclonal Antibodies ◽  
Erythrocyte Ghosts ◽  
Con A ◽  
Down Regulation ◽  
Regulation Of Expression ◽  
Variable Effect

We have previously shown that the In(Lu) gene down-regulates expression of an erythrocyte protein antigen identified by murine monoclonal antibody (MoAb) A3D8. In the present study we have examined In(Lu) Lu(a- b-) erythrocytes for expression of additional epitopes on the erythrocyte 80 kilodalton protein (p80) bearing the A3D8 antigen. Using a total of seven additional MoAbs that recognize three epitopes on erythrocyte p80, we have shown that In(Lu) Lu(a-b-) erythrocytes exhibit down-regulation of expression of all three epitopes. In(Lu) erythrocytes also showed a reduction in their reactivity to rabbit antibodies produced against purified p80 from either erythrocytes or lymphocytes. Furthermore the reactivity of the MoAbs was not altered by treatment of the cells with neuraminidase but was substantially reduced by treatment of cells with trypsin or chymotrypsin. The polyclonal anti- p80 sera were shown to react with a fragment of 50,000 daltons, still associated with erythrocyte ghosts, following treatment of the cells with trypsin or chymotrypsin. Treatment of erythrocytes with the thiol- reactive reagent AET decreased their reactivity with the MoAbs but had a variable effect on their reactivity with polyclonal antibodies. Erythrocyte p80 is a glycoprotein with N-linked oligosaccharides, as demonstrated by its binding to concanavalin A (Con A) and Len culinaris lectins. Following Endoglycosidase F treatment, erythrocyte p80 underwent a reduction in apparent mol wt of 11,000. The presence of a reduced amount of an intact p80 glycoprotein, seen by a decrease in reactivity with MoAbs directed at three distinct epitopes and with two different polyclonal antibodies, suggests that the In(Lu) gene interferes with expression by erythrocytes of the entire p80 glycoprotein.

scholarly journals A shortened variant of red cell membrane protein 4.1

Blood ◽  
1982 ◽  
Vol 60 (1) ◽  
pp. 265-267 ◽  
Author(s):  
N Alloisio ◽  
E Dorleac ◽  
J Delaunay ◽  
R Girot ◽  
C Galand ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Membrane ◽  
Membrane Protein ◽  
Phosphorylation Site ◽  
Red Cell ◽  
Heterozygous State ◽  
Red Cell Membrane ◽  
Protein 4.1 ◽  
Protein 4.2 ◽  
Cell Membrane Protein

Abstract In a healthy 32-yr-old woman with normal red cell morphology, a shortened variant of cytoskeletal membrane protein 4.1 is described at the heterozygous state. One haploid set of protein 4.1 migrates below protein 4.2 and displays a reduction in mass of approximately 8500 with regard to the normal haploid set. The shortening corresponds to a deletion of about 75 amino acids and concerns both subcomponents a and b of protein 4.1. It seems to involve some phosphorylation site(s). It was transmitted to the proposita's son (who inherited elliptocytosis with band 4.1 deficiency from his father). To our knowledge, the present abnormality is the first unequivocal variant of erythrocyte membrane protein 4.1 recognized up to now.

Cloning and characterization of cDNAs coding for the heavy and light chains of a monoclonal antibody specific for Pseudomonas aeruginosa outer membrane protein I

Gene ◽  
1988 ◽  
Vol 74 (2) ◽  
pp. 335-345 ◽  
Author(s):  
Matthias Marge ◽  
Ansley Eckhardt ◽  
Werner Ehret ◽  
Bernd-Ulrich von Specht ◽  
Michael Buchêne ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Light Chains
Sign in / Sign up

Export Citation Format

Share Document