Conservation of epitopes recognized by monoclonal antibodies against the separated subunits of influenza hemagglutinin among type A viruses of the same and different subtypes

1991 ◽  
Vol 116 (1-4) ◽  
pp. 285-292 ◽  
Author(s):  
Alicia Sanchez-Fauquier ◽  
Matilde Guillen ◽  
J. Martin ◽  
A. P. Kendal ◽  
J. A. Melero
Keyword(s):  
Monoclonal Antibodies ◽  
Type A ◽  
Influenza Hemagglutinin

scholarly journals CGRP-antibodies, topiramate and botulinum toxin type A in episodic and chronic migraine: A systematic review and meta-analysis

Cephalalgia ◽  
2021 ◽  
pp. 033310242110181
Author(s):  
Florian Frank ◽  
Hanno Ulmer ◽  
Victoria Sidoroff ◽  
Gregor Broessner
Keyword(s):  
Systematic Review ◽  
Monoclonal Antibodies ◽  
Botulinum Toxin ◽  
Response Rate ◽  
Meta Analysis ◽  
Botulinum Toxin Type A ◽  
Type A ◽  
Response Rates ◽  
Botulinum Toxin Type ◽  
Odds Ratios

Background The approval of monoclonal antibodies for prevention of migraine has revolutionized treatment for patients. Oral preventatives are still considered first line treatments as head-to-head trials comparing them with antibodies are lacking. Methods The main purpose of this study was to provide a comparative overview of the efficacy of three commonly prescribed migraine preventative medication classes. For this systematic review and meta-analysis, we searched the databases CENTRAL, EMBASE, and MEDLINE until 20 March 2020. We included RCTs reporting the 50% response rates for topiramate, Botulinum Toxin Type A and monoclonal antibodies against CGRP(r). Studies were excluded if response rates were not reported, treatment allocation was unclear, or if study quality was insufficient. Primary outcome measure were the 50% response rates. The pooled odds ratios with 95% confidence intervals were calculated with the random effects model. The study was registered at PROSPERO (CRD42020222880). Findings We identified 6552 reports. Thirty-two were eligible for our review. Studies assessing monoclonal antibodies included 13,302 patients and yielded pooled odds ratios for the 50% response rate of 2.30 (CI: 2.11–2.50). Topiramate had an overall effect estimate of 2.70 (CI: 1.97–3.69) with 1989 included patients and Botulinum Toxin Type A achieved 1.28 (CI: 0.98–1. 67) with 2472 patients included. Interpretation Topiramate, botulinum toxin type A and monoclonal antibodies showed higher odds ratios in achieving a 50% response rate compared to placebo. Topiramate numerically demonstrated the greatest effect size but also the highest drop-out rate.

Optimization of stereospecific targeting technique for selective production of monoclonal antibodies against native ephrin type-A receptor 2

2020 ◽  
Vol 484-485 ◽  
pp. 112813
Author(s):  
Yasuhiro Yamasaki ◽  
Chiho Miyamae ◽  
Yushi Isozaki ◽  
Keisuke Ichikawa ◽  
Yoshiki Kaneko ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Type A

scholarly journals Characterization of Neutralizing Antibodies and Identification of Neutralizing Epitope Mimics on the Clostridium botulinum Neurotoxin Type A

2001 ◽  
Vol 67 (7) ◽  
pp. 3201-3207 ◽  
Author(s):  
Han-Chung Wu ◽  
Chia-Tsui Yeh ◽  
Yue-Ling Huang ◽  
Lih-Jeng Tarn ◽  
Chien-Cheng Lung
Keyword(s):  
Monoclonal Antibodies ◽  
Neutralizing Antibodies ◽  
Clostridium Botulinum ◽  
Neuromuscular Junctions ◽  
Competitive Inhibition ◽  
Lethal Dose ◽  
Humoral Response ◽  
Type A ◽  
Phage Clone ◽  
Neutralizing Epitopes

ABSTRACT Clostridium botulinum neurotoxin type A (BTx-A) is known to inhibit the release of acetylcholine at the neuromuscular junctions and synapses and to cause neuroparalysis and death. In this study, we have identified two monoclonal antibodies, BT57-1 and BT150-3, which protect ICR mice against lethal doses of BTx-A challenge. The neutralizing activities for BT57-1 and BT150-3 were 103 and 104 times the 50% lethal dose, respectively. Using immunoblotting analysis, BT57-1 was recognized as a light chain and BT150-3 was recognized as a heavy chain of BTx-A. Also, applying the phage display method, we investigated the antibodies' neutralizing B-cell epitopes. These immunopositive phage clones displayed consensus motifs, Asp-Pro-Leu for BT57-1 and Cys-X-Asp-Cys for BT150. The synthetic peptide P4M (KGTFDPLQEPRT) corresponded to the phage-displayed peptide selected by BT57-1 and was able to bind the antibodies specifically. This peptide was also shown by competitive inhibition assay to be able to inhibit phage clone binding to BT57-1. Aspartic acid (D5) in P4M was crucial to the binding of P4M to BT57-1, since its binding activity dramatically decreased when it was changed to lysine (K5). Finally, immunizing mice with the selected phage clones elicited a specific humoral response against BTx-A. These results suggest that phage-displayed random-peptide libraries are useful in identifying the neutralizing epitopes of monoclonal antibodies. In the future, the identification of the neutralizing epitopes of BTx-A may provide important information for the identification of the BTx-A receptor and the design of a BTx-A vaccine.

scholarly journals Cytotoxic T lymphocyte recognition of the influenza hemagglutinin gene product expressed by DNA-mediated gene transfer.

1984 ◽  
Vol 159 (2) ◽  
pp. 341-354 ◽  
Author(s):  
T J Braciale ◽  
V L Braciale ◽  
T J Henkel ◽  
J Sambrook ◽  
M J Gething
Keyword(s):  
Gene Transfer ◽  
Gene Product ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Type A ◽  
Target Antigen ◽  
Influenza Hemagglutinin ◽  
Ha Gene ◽  
Hemagglutinin Gene ◽  
Target Molecules

We have used the technique of DNA-mediated gene transfer to examine cytotoxic T lymphocyte (CTL) recognition of the product of the cloned A/JAPAN/305/57 hemagglutinin (HA) gene in murine (L929) cells. Using both heterogeneous and homogeneous (clonal) populations of type A influenza-specific CTL, we have demonstrated that the HA molecule can serve as a target antigen for both the subtype-specific and the cross-reactive subpopulations of influenza-specific CTL. Our results also raise the possibility that other virus-specified polypeptides may serve as target molecules for cross-reactive CTL.

scholarly journals The bat influenza H17N10 can be neutralized by broadly-neutralizing monoclonal antibodies and its neuraminidase can facilitate viral egress.

2018 ◽  
Author(s):  
George Carnell ◽  
Efstathios Giotis ◽  
Keith Grehan ◽  
Francesca Ferrara ◽  
Stuart Mather ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Envelope Glycoprotein ◽  
Human Population ◽  
Influenza A ◽  
Cellular Receptor ◽  
Zoonotic Potential ◽  
Safety Issues ◽  
Influenza Hemagglutinin ◽  
Viral Egress ◽  
Cell Supernatant

The diversity of subtypes within the Influenza A virus genus has recently expanded with the identification of H17N10 and H18N11 from bats. In order to further study the tropism and zoonotic potential of these viruses, we have successfully produced lentiviral pseudotypes bearing both H17 and N10. These pseudotypes were shown to be efficiently neutralized by the broadly-neutralizing monoclonal antibodies CR9114 and FI6. Our studies also confirm previous reports that H17 does not use sialic acid as its cellular receptor, as pseudotypes bearing the H17 envelope glycoprotein are released into the cell supernatant in the absence of neuraminidase. However, we demonstrate that N10 facilitates heterosubtypic (H5 and H7) influenza hemagglutinin-bearing pseudotype release in the absence of another source of neuraminidase, significantly increasing luciferase pseudotype production titres. Despite this, N10 shows no activity in the enzyme-linked lectin assay used for traditional sialidases. These findings suggest that this protein plays an important role in viral egress, but is perhaps involved in further accessory roles in the bat influenza lifecycle that are yet to be discovered. Thus we show the lentiviral pseudotype system is a useful research tool, and amenable for investigation of bat influenza tropism, restriction and sero-epidemiology, without the constraints or safety issues with producing a replication-competent virus, to which the human population is naive.

Characterization of Monoclonal Antibodies to Botulinum Type A Neurotoxin

1993 ◽  
pp. 433-436 ◽  
Author(s):  
Bassam Hallis ◽  
Sarah Fooks ◽  
Clifford Shone ◽  
Peter Hambleton
Keyword(s):  
Monoclonal Antibodies ◽  
Type A ◽  
Botulinum Type
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