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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
by
Yin, Yuncong
, Yang, Zengqi
, Rehman, Zaib Ur
, Shi, Mengyu
, Sun, Yingjie
, Meng, Chunchun
, Yang, Bin
, Ding, Chan
, Ren, Shanhui
, Liu, Panrao
, Gao, Xiaolong
, Qu, Yurong
in
Apoptosis
/ Autophagy
/ Avian orthoavulavirus 1
/ biogenesis
/ Biosynthesis
/ Cooperation
/ Cytochrome
/ Endoplasmic reticulum
/ energy
/ enzymes
/ Genetic aspects
/ giant cells
/ Glycoproteins
/ Homeostasis
/ Immunology
/ Lectins
/ Life Sciences
/ Medicine
/ Medicine & Public Health
/ Microbiology
/ Mitochondria
/ Morphology
/ Newcastle disease
/ Pathogenic microorganisms
/ Plasmids
/ Proteins
/ Quality control
/ Short Report
/ Trends
/ unfolded protein response
/ Veterinary Medicine/Veterinary Science
/ Virology
/ virulence
/ Virulence (Microbiology)
/ Viruses
2019
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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
by
Yin, Yuncong
, Yang, Zengqi
, Rehman, Zaib Ur
, Shi, Mengyu
, Sun, Yingjie
, Meng, Chunchun
, Yang, Bin
, Ding, Chan
, Ren, Shanhui
, Liu, Panrao
, Gao, Xiaolong
, Qu, Yurong
in
Apoptosis
/ Autophagy
/ Avian orthoavulavirus 1
/ biogenesis
/ Biosynthesis
/ Cooperation
/ Cytochrome
/ Endoplasmic reticulum
/ energy
/ enzymes
/ Genetic aspects
/ giant cells
/ Glycoproteins
/ Homeostasis
/ Immunology
/ Lectins
/ Life Sciences
/ Medicine
/ Medicine & Public Health
/ Microbiology
/ Mitochondria
/ Morphology
/ Newcastle disease
/ Pathogenic microorganisms
/ Plasmids
/ Proteins
/ Quality control
/ Short Report
/ Trends
/ unfolded protein response
/ Veterinary Medicine/Veterinary Science
/ Virology
/ virulence
/ Virulence (Microbiology)
/ Viruses
2019
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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
by
Yin, Yuncong
, Yang, Zengqi
, Rehman, Zaib Ur
, Shi, Mengyu
, Sun, Yingjie
, Meng, Chunchun
, Yang, Bin
, Ding, Chan
, Ren, Shanhui
, Liu, Panrao
, Gao, Xiaolong
, Qu, Yurong
in
Apoptosis
/ Autophagy
/ Avian orthoavulavirus 1
/ biogenesis
/ Biosynthesis
/ Cooperation
/ Cytochrome
/ Endoplasmic reticulum
/ energy
/ enzymes
/ Genetic aspects
/ giant cells
/ Glycoproteins
/ Homeostasis
/ Immunology
/ Lectins
/ Life Sciences
/ Medicine
/ Medicine & Public Health
/ Microbiology
/ Mitochondria
/ Morphology
/ Newcastle disease
/ Pathogenic microorganisms
/ Plasmids
/ Proteins
/ Quality control
/ Short Report
/ Trends
/ unfolded protein response
/ Veterinary Medicine/Veterinary Science
/ Virology
/ virulence
/ Virulence (Microbiology)
/ Viruses
2019
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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
Journal Article
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
2019
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Overview
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
mt
. 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.
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