Avian Influenza A Nucleoprotein Antigen Capture ELISA Kit

Name: Avian Influenza A Nucleoprotein Antigen Capture ELISA Kit
SKU: DEIA2026
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Complex sample matrices

Species Reactivity

Universal

Detection Method

sELISA

Intended Use

This kit is a highly sensitive and specific enzyme immunoassay for the detection of Influenza A nucleoprotein antigen in complex sample matrices derived from both human and veterinary sources.

Contents of Kit

1. Antigen Capture Plate (96 tests) 2 each
2. Sample Preparation Reagent (1×) 12 ml
3. Positive Control (1×) 1 ml
4. Negative Control (1×) 2×1.5 ml
5. Wash Buffer (20×) 50 ml
6. Detection Antibody, HRP-labeled (1×) 22 ml
7. Chromagen Solution (1×) 22 ml
8. Stop Solution (1×) 22 ml
9. Sample Dilution Tray 2 each

Storage

Store all kit components at 2 - 8 °C. Crystal formation may occur in the wash buffer concentrate during prolonged storage at 2 - 8°C

General Description

Influenza virus nucleoprotein (NP) is a structural protein which encapsidates the negative strand viral RNA. NP is one of the main determinants of species specificity. The question of how far the NP gene can cross the species barrier by reassortment and become adapted by mutation to the new host has been discussed.

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Molecular Basis of the Ternary Interaction between NS1 of the 1918 Influenza A Virus, PI3K, and CRK

VIRUSES-BASEL

Authors: Dubrow, Alyssa; Lin, Sirong; Savage, Nowlan; Shen, Qingliang; Cho, Jae-Hyun

Abstract

The 1918 influenza A virus (IAV) caused the worst flu pandemic in human history. Non-structural protein 1 (NS1) is an important virulence factor of the 1918 IAV and antagonizes host antiviral immune responses. NS1 increases virulence by activating phosphoinositide 3-kinase (PI3K) via binding to the p85 beta subunit of PI3K. Intriguingly, unlike the NS1 of other human IAV strains, 1918 NS1 hijacks another host protein, CRK, to form a ternary complex with p85 beta, resulting in hyperactivation of PI3K. However, the molecular basis of the ternary interaction between 1918 NS1, CRK, and PI3K remains elusive. Here, we report the structural and thermodynamic bases of the ternary interaction. We find that the C-terminal tail (CTT) of 1918 NS1 remains highly flexible in the complex with p85 beta. Thus, the CTT of 1918 NS1 in the complex with PI3K can efficiently hijack CRK. Notably, our study indicates that 1918 NS1 enhances its affinity to p85 beta in the presence of CRK, which might result in enhanced activation of PI3K. Our results provide structural insight into how 1918 NS1 hijacks two host proteins simultaneously.

Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Authors: Cho, Jae-Hyun; Zhao, Baoyu; Shi, Jie; Savage, Nowlan; Shen, Qingliang; Byrnes, James; Yang, Lin; Hwang, Wonmuk; Li, Pingwei

Abstract

The 1918 influenza A virus (IAV) caused the most severe flu pandemic in recorded human history. Nonstructural protein 1 (NS1) is an important virulence factor of the 1918 IAV. NS1 antagonizes host defense mechanisms through interactions with multiple host factors. One pathway by which NS1 increases virulence is through the activation of phosphoinositide 3-kinase (PI3K) by binding to its p85 beta subunit. Here we present the mechanism underlying the molecular recognition of the p85 beta subunit by 1918 NS1. Using X-ray crystallography, we determine the structure of 1918 NS1 complexed with p85 beta of human PI3K. We find that the 1918 NS1 effector domain (1918 NS1(ED)) undergoes a conformational change to bind p85 beta. Using NMR relaxation dispersion and molecular dynamics simulation, we identify that free 1918 NS1(ED) exists in a dynamic equilibrium between p85 beta-binding-competent and -incompetent conformations in the sub-millisecond timescale. Moreover, we discover that NS1(ED) proteins of 1918 (H1N1) and Udorn (H3N2) strains exhibit drastically different conformational dynamics and binding kinetics to p85 beta. These results provide evidence of strain-dependent conformational dynamics of NS1. Using kinetic modeling based on the experimental data, we demonstrate that 1918 NS1(ED) can result in the faster hijacking of p85 beta compared to Ud NS1(ED), although the former has a lower affinity to p85 beta than the latter. Our results suggest that the difference in binding kinetics may impact the competition with cellular antiviral responses for the activation of PI3K. We anticipate that our findings will increase the understanding of the strain-dependent behaviors of influenza NS1 proteins.