Hemagglutinin-neuraminidase and fusion proteins of virulent Newcastle disease virus cooperatively disturb fusion-fission homeostasis to enhance mitochondrial function by activating the unfolded protein response of endoplasmic reticulum and mitochondrial stress

• Published in: Veterinary research (Paris) Vol. 50; no. 1; p. 37
• Main Authors: Ren, Shanhui, Rehman, Zaib Ur, Shi, Mengyu, Yang, Bin, Liu, Panrao, Yin, Yuncong, Qu, Yurong, Meng, Chunchun, Yang, Zengqi, Gao, Xiaolong, Sun, Yingjie, Ding, Chan
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 22.05.2019; BioMed Central; BMC
• Subjects: Apoptosis; Autophagy; Biosynthesis; Cooperation; Cytochrome; Endoplasmic reticulum; Genetic aspects; Glycoproteins; Homeostasis; Lectins; Life Sciences; Mitochondria; Morphology; Newcastle disease; Pathogenic microorganisms; Plasmids; Proteins; Quality control; Short Report; Trends; Virulence (Microbiology); Viruses
• ISSN: 1297-9716; 0928-4249; 1297-9716
• DOI: 10.1186/s13567-019-0654-y

The fusogenically activated F and HN proteins of virulent NDV induce complete autophagic flux in DF-1 and A549 cells. However, the effect of both glycoproteins on mitochondria remains elusive. Here, we found that F and HN cooperation increases mitochondrial biogenesis but does not cause the mitochondria damage. We observed that both glycoproteins change the morphological characteristics and spatial distribution of intracellular mitochondria. F and HN cooperate cooperatively to induce ER stress and UPR . Our preliminary data suggested that F and HN cooperatively disturb mitochondrial fusion-fission homeostasis to enhance mitochondrial biogenesis, and eventually meet the energy demand of syncytium formation.