Marine Morbilliviruses: Diversity and Interaction with Signaling Lymphocyte Activation Molecules

Kazue Ohishi1, Tadashi Maruyama2, Fumio Seki3

  • 1Faculty of Engineering, Tokyo Polytechnic University, 1583, Iiyama, Atsugi, Kanagawa 243-0297, Japan. cie20910@syd.odn.ne.jp.

Viruses
|July 7, 2019
PubMed

Insights

Marine morbilliviruses like phocine distemper virus (PDV) and cetacean morbillivirus (CeMV) interact with the SLAM receptor. Understanding these interactions is key to predicting viral host specificity and potential host switching events.

Area of Science:

  • Marine virology
  • Immunology
  • Structural biology

Background:

  • Phocine distemper virus (PDV) and cetacean morbillivirus (CeMV) are marine morbilliviruses with significant epidemiological impact.
  • The signaling lymphocyte activation molecule (SLAM) is the primary cellular receptor for these viruses.

Purpose of the Study:

  • To review the interaction between marine morbilliviruses (PDV and CeMV) and their cellular receptor, SLAM.
  • To elucidate the structural basis of viral tropism and host specificity.

Main Methods:

  • Analysis of three-dimensional crystal structures and homology models of SLAM.
  • In silico analysis of viral hemagglutinin (H) protein and SLAM interactions.
  • Integration of epidemiological, virological, structural, and computational data.

Main Results:

  • 35 key residues in SLAM are crucial for binding the morbillivirus H protein and determining viral tropism.
  • These residues are highly conserved in pinnipeds, suggesting PDV's potential to infect them.
  • Less conserved SLAM residues in cetaceans suggest broader CeMV-H protein specificity for infecting diverse whale species and potentially seals.

Conclusions:

  • SLAM-morbillivirus H protein interactions are critical for host specificity.
  • Structural and computational analyses reveal complex residue interactions governing viral tropism.
  • Integrating diverse study types offers insights into marine morbillivirus host switching.

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