Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate–protein ligase A

2020 ◽  
Vol 117 (12) ◽  
pp. 3677-3687
Author(s):  
Xinyi Zhang ◽  
Jinglei Nie ◽  
Yuanmin Zheng ◽  
Jie Ren ◽  
An‐Ping Zeng
Keyword(s):  
Multifunctional Enzyme ◽  
H Protein

scholarly journals Genetic diversity of the attachment (H) protein gene of current field isolates of canine distemper virus.

1997 ◽  
Vol 78 (2) ◽  
pp. 367-372 ◽  
Author(s):  
G Bolt ◽  
P Arctander ◽  
T D Jensen ◽  
M J Appel ◽  
E Gottschalck ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Canine Distemper Virus ◽  
Protein Gene ◽  
Canine Distemper ◽  
Current Field ◽  
Field Isolates ◽  
H Protein

Molecular mechanism of the multifunctional enzyme l-δ-(α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) synthetase

1995 ◽  
Vol 23 (4) ◽  
pp. 629S-629S ◽  
Author(s):  
CHIA-YANG SHIAU ◽  
MICHAEL F. BYFORD ◽  
JACK E. BALDWIN ◽  
CHRISTOPHER J. SCHOFIELD
Keyword(s):  
Molecular Mechanism ◽  
Multifunctional Enzyme

scholarly journals PPARα Activation Induces N ε-Lys-Acetylation of Rat Liver Peroxisomal Multifunctional Enzyme Type 1

Lipids ◽  
2013 ◽  
Vol 49 (2) ◽  
pp. 119-131 ◽  
Author(s):  
Miguel A. Contreras ◽  
Oscar Alzate ◽  
Avtar K. Singh ◽  
Inderjit Singh
Keyword(s):  
Rat Liver ◽  
Multifunctional Enzyme

scholarly journals Corrigendum to “Interaction between goniothalamin and peroxisomal multifunctional enzyme type 2 triggering endoplasmic reticulum stress” [Heliyon 6 (10) (October 2020) e05200]

Heliyon ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. e05907
Author(s):  
Thanet Sophonnithiprasert ◽  
Ornjira Aruksakunwong ◽  
Etsu Tashiro ◽  
Yasumitsu Kondoh ◽  
Makoto Muroi ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Multifunctional Enzyme

Crystallization and characterization of the dehydrogenase domain from rat peroxisomal multifunctional enzyme type 1

2002 ◽  
Vol 58 (4) ◽  
pp. 690-693 ◽  
Author(s):  
Jukka P. Taskinen ◽  
Tiila-Riikka Kiema ◽  
Kari T. Koivuranta ◽  
Rik K. Wierenga ◽  
J. Kalervo Hiltunen
Keyword(s):  
Multifunctional Enzyme

Short-stalk isoforms of CADM1 and CADM2 trigger neuropathogenic measles virus-mediated membrane fusion by interacting with the viral hemagglutinin

2021 ◽  
Author(s):  
Ryuichi Takemoto ◽  
Tateki Suzuki ◽  
Takao Hashiguchi ◽  
Yusuke Yanagi ◽  
Yuta Shirogane
Keyword(s):  
Cell Membrane ◽  
Membrane Fusion ◽  
Measles Virus ◽  
Subacute Sclerosing Panencephalitis ◽  
Febrile Illness ◽  
Host Factors ◽  
F Protein ◽  
Short Stalk ◽  
Head Domain ◽  
H Protein

Measles virus (MeV), an enveloped RNA virus in the family Paramyxoviridae , usually causes acute febrile illness with skin rash, but in rare cases persists in the brain, causing a progressive neurological disorder, subacute sclerosing panencephalitis (SSPE). MeV bears two envelope glycoproteins, the hemagglutinin (H) and fusion (F) proteins. The H protein possesses a head domain that initially mediates receptor binding and a stalk domain that subsequently transmits the fusion-triggering signal to the F protein. We have recently shown that cell adhesion molecule 1 (CADM1, also known as IGSF4A, Necl-2, SynCAM1) and CADM2 (also known as IGSF4D, Necl-3, SynCAM2) are host factors enabling cell-cell membrane fusion mediated by hyperfusogenic F proteins of neuropathogenic MeVs as well as MeV spread between neurons lacking the known receptors. CADM1 and CADM2 interact in cis with the H protein on the same cell membrane, triggering hyperfusogenic F protein-mediated membrane fusion. Multiple isoforms of CADM1 and CADM2 containing various lengths of their stalk regions are generated by alternative splicing. Here we show that only short-stalk isoforms of CADM1 and CADM2 predominantly expressed in the brain induce hyperfusogenic F protein-mediated membrane fusion. While the known receptors interact in trans with the H protein through its head domain, these isoforms can interact in cis even with the H protein lacking the head domain and trigger membrane fusion, presumably through its stalk domain. Thus, our results unveil a new mechanism of viral fusion triggering by host factors. Importance Measles, an acute febrile illness with skin rash, is still an important cause of childhood morbidity and mortality worldwide. Measles virus (MeV), the causative agent of measles, may also cause a progressive neurological disorder, subacute sclerosing panencephalitis (SSPE), several years after acute infection. The disease is fatal, and no effective therapy is available. Recently, we have reported that cell adhesion molecule 1 (CADM1) and CADM2 are host factors enabling MeV cell-to-cell spread in neurons. These molecules interact in cis with the MeV attachment protein on the same cell membrane, triggering the fusion protein and causing membrane fusion. CADM1 and CADM2 are known to exist in multiple splice isoforms. In this study, we report that their short-stalk isoforms can induce membrane fusion by interacting in cis with the viral attachment protein independently of its receptor-binding head domain. This finding may have important implications for cis -acting fusion triggering by host factors.

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