EMC Abstracts

Official abstracts site for the European Microscopy Congress

MENU 
  • Home
  • Meetings Archive
    • The 16th European Microscopy Congress 2016
  • Keyword Index
  • Your Favorites
    • Favorites
    • Login
    • Register
    • View and Print All Favorites
    • Clear all your favorites
  • Advanced Search

Structural characterization of the protein P2, the aphid transmission factor of the cauliflower mosaic virus

Abstract number: 6880

Session Code: LS06-074

DOI: 10.1002/9783527808465.EMC2016.6880

Meeting: The 16th European Microscopy Congress 2016

Session: Life Sciences

Topic: Host-pathogen Interactions

Presentation Form: Poster

Corresponding Email: lecorre@cbs.cnrs.fr

Francois Lecorre (1), Joséphine Lai Kee Him (1)

1. Multi-scale structural biology, Centre de Biochimie Structurale, Montpellier, France

Keywords: aphid, coiled-coil, plant, protein, virus

Cauliflower mosaic virus (CaMV) is transmitted from plant to plant through an interaction with aphid vectors, according to a non-circulant transmission (1). Until recently, it was admitted that CaMV transmission was not specific. However, our colleagues have recently identified a proteic receptor at the extreme tip of the aphid maxillary stylets involved in interaction with the viral protein P2, the transmission factor of  CaMV, suggesting a specific and complex interaction process (2).

As a consequence, it is now believed that  CaMV transmission involves an aphid receptor and two viral proteins, P2 and P3. P2 binds both to the aphid receptor and to P3, which is tightly associated with the CaMV viral particle, forming the transmissible viral complex (Figure 1). We have previously resolved the P3 structure by X-ray crystallography (3) and proposed a model  for the CaMV:P3 complex based on single particle cryo-electron microscopy (cryo-EM) studies (4). We are now trying to characterize P2, the viral helper-component, which acts as a bridge between the aphid receptor and the viral complex CaMV:P3, thus playing a major role in plant-vector transmission. Structure predictions indicate that P2 is composed by a N-terminal globular domain, followed by two coiled-coil domains. Due to the presence of these coiled-coil domains which seem to confer the protein a strong tendency to aggregate, it is extremely difficult to work and manipulate the native P2 protein. Hence, we have adopted a hybrid strategy combining  X-ray crystallography and cryo-EM studies to investigate the structural organization of P2. In this context, we are trying to crystallize various domains of the P2 protein over-expressed in bacteria. Additionally, we want to obtain the tertiary structure of P2 by using electron microscopy. Indeed, as His-tagged P2 protein can form paracrystals when expressed in sf9 cells (Figure 2), we use  cryo-electron tomography  and sub-tomogram averaging methods to get first structural data on P2 and interactions between coiled-coil domains. Moreover, a P2 mutant (157m) was shown to decorate microtubules in sf9 cells (Figure 3). We defined conditions of purification and used these decorated microtubules to engage a single particle analysis in cryo-EM and image processing.

This poster presents the first structural results in the organization of the P2 protein and its multiple interactions.

(1)    Martinière et al., Plant Signaling & Behavior, 4:6, 548-550, 2009

(2)    Uzest et al., PNAS, vol. 104 no. 46, 17959-17964, 2007

(3)    Hoh et al., Journal of Virology, vol. 84 no. 9, 4706-4713, 2010

(4)    Plisson et al., J. Mol. Biol, 346:267-277, 2005

Figures:

CaMV transmission to aphids

P2 paracrystals in Sf9 cells

P2 mutant (157m) decorating sf9 cell microtubules

To cite this abstract:

Francois Lecorre, Joséphine Lai Kee Him; Structural characterization of the protein P2, the aphid transmission factor of the cauliflower mosaic virus. The 16th European Microscopy Congress, Lyon, France. https://emc-proceedings.com/abstract/structural-characterization-of-the-protein-p2-the-aphid-transmission-factor-of-the-cauliflower-mosaic-virus/. Accessed: April 20, 2021
  • Tweet
  • Email
  • Print
Save to PDF

« Back to The 16th European Microscopy Congress 2016

EMC Abstracts - https://emc-proceedings.com/abstract/structural-characterization-of-the-protein-p2-the-aphid-transmission-factor-of-the-cauliflower-mosaic-virus/

Most Viewed Abstracts

  • mScarlet, a novel high quantum yield (71%) monomeric red fluorescent protein with enhanced properties for FRET- and super resolution microscopy
  • 3D structure and chemical composition reconstructed simultaneously from HAADF-STEM images and EDS-STEM maps
  • Pixelated STEM detectors: opportunities and challenges
  • Layer specific optical band gap measurement at nanoscale in MoS2 and ReS2 van der Waals compounds by high resolution electron energy loss spectroscopy
  • Atomic relaxation in ultrathin fcc metal nanowires

Your Favorites

You can save and print a list of your favorite abstracts by clicking the “Favorite” button at the bottom of any abstract. View your favorites »

Visit Our Partner Sites

The 16th European Microscopy Congress

The official web site of the 16th European Microscopy Congress.

European Microscopy Society

European Microscopy Society logoThe European Microscopy Society (EMS) is committed to promoting the use and the quality of advanced microscopy in all its aspects in Europe.

International Federation of Societies for Microscopy

International Federation of Societies for Microscopy logoThe IFSM aims to contribute to the advancement of microscopy in all its aspects.

Société Française des Microscopies

Société Française des MicroscopiesThe Sfµ is a multidisciplinary society which aims to improve and spread the knowledge about Microscopy.

Connect with us

Imaging & Microscopy
Official Media Partner of the European Microscopy Society.

  • Help & Support
  • About Us
  • Cookies & Privacy
  • Wiley Job Network
  • Terms & Conditions
  • Advertisers & Agents
Copyright © 2021 John Wiley & Sons, Inc. All Rights Reserved.
Wiley
loading Cancel
Post was not sent - check your email addresses!
Email check failed, please try again
Sorry, your blog cannot share posts by email.
This site uses cookies: Find out more.