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Review
. 2019 Aug 8;11(8):729.
doi: 10.3390/v11080729.

Host Cellular Receptors for the Peste des Petits Ruminant Virus

Meera Prajapati  1 , Niyokwishimira Alfred  1 , Yongxi Dou  1 , Xiangping Yin  1 , Raju Prajapati  2 , Yanmin Li  1 , Zhidong Zhang  3   4
Affiliations
Review

Host Cellular Receptors for the Peste des Petits Ruminant Virus

Meera Prajapati et al. Viruses. .

Abstract

Peste des Petits Ruminant (PPR) is an important transboundary, OIE-listed contagious viral disease of primarily sheep and goats caused by the PPR virus (PPRV), which belongs to the genus Morbillivirus of the family Paramyxoviridae. The mortality rate is 90-100%, and the morbidity rate may reach up to 100%. PPR is considered economically important as it decreases the production and productivity of livestock. In many endemic poor countries, it has remained an obstacle to the development of sustainable agriculture. Hence, proper control measures have become a necessity to prevent its rapid spread across the world. For this, detailed information on the pathogenesis of the virus and the virus host interaction through cellular receptors needs to be understood clearly. Presently, two cellular receptors; signaling lymphocyte activation molecule (SLAM) and Nectin-4 are known for PPRV. However, extensive information on virus interactions with these receptors and their impact on host immune response is still required. Hence, a thorough understanding of PPRV receptors and the mechanism involved in the induction of immunosuppression is crucial for controlling PPR. In this review, we discuss PPRV cellular receptors, viral host interaction with cellular receptors, and immunosuppression induced by the virus with reference to other Morbilliviruses.

Keywords: Morbillivirus; Nectin-4; PPRV; SLAM.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Cartoon and solvent drawing of the predicted PPRV H-SLAM complex. The complexes of the H protein’s six-bladed β-propeller head domain and the receptor SLAM V-like were built, in which β4–β6 of the head domain and the typical β-sandwich structure of the V domain were interacting surfaces. (A and B) show the analysis of the hydrophobicity of PPRV H and sheep SLAM, indicating that there was a strong hydrophobic groove between β4–β6 on the H head domain, and the surface on the sheep SLAM had stronger hydrophobicity. (C) A structure comparison revealed that the PPRV H-sheep SLAM and PPRV H-human SLAM complexes are very similar. (D) Interaction patterns between PPRV H and human SLAM.
See this image and copyright information in PMC

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