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  • Nature Publishing Group (NPG)  (5)
  • International Union of Crystallography (IUCr)  (3)
  • The American Society for Microbiology (ASM)  (2)
  • 1
    Publication Date: 2013-07-09
    Description: The newly emergent Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe pulmonary disease in humans, representing the second example of a highly pathogenic coronavirus, the first being SARS-CoV. CD26 (also known as dipeptidyl peptidase 4, DPP4) was recently identified as the cellular receptor for MERS-CoV. The engagement of the MERS-CoV spike protein with CD26 mediates viral attachment to host cells and virus-cell fusion, thereby initiating infection. Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Furthermore, binding between the RBD and CD26 is measured using real-time surface plasmon resonance with a dissociation constant of 16.7 nM. The viral RBD is composed of a core subdomain homologous to that of the SARS-CoV spike protein, and a unique strand-dominated external receptor binding motif that recognizes blades IV and V of the CD26 beta-propeller. The atomic details at the interface between the two binding entities reveal a surprising protein-protein contact mediated mainly by hydrophilic residues. Sequence alignment indicates, among betacoronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Guangwen -- Hu, Yawei -- Wang, Qihui -- Qi, Jianxun -- Gao, Feng -- Li, Yan -- Zhang, Yanfang -- Zhang, Wei -- Yuan, Yuan -- Bao, Jinku -- Zhang, Buchang -- Shi, Yi -- Yan, Jinghua -- Gao, George F -- England -- Nature. 2013 Aug 8;500(7461):227-31. doi: 10.1038/nature12328. Epub 2013 Jul 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23831647" target="_blank"〉PubMed〈/a〉
    Keywords: Conserved Sequence/genetics ; Coronavirus/*chemistry/genetics/*metabolism ; Dipeptidyl Peptidase 4/*chemistry/metabolism ; Humans ; Protein Binding ; Protein Interaction Domains and Motifs/genetics ; Protein Structure, Tertiary/genetics ; Receptors, Virus/*chemistry/*metabolism ; *Virus Attachment
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2013-04-05
    Description: Current human immunodeficiency virus-1 (HIV-1) vaccines elicit strain-specific neutralizing antibodies. However, cross-reactive neutralizing antibodies arise in approximately 20% of HIV-1-infected individuals, and details of their generation could provide a blueprint for effective vaccination. Here we report the isolation, evolution and structure of a broadly neutralizing antibody from an African donor followed from the time of infection. The mature antibody, CH103, neutralized approximately 55% of HIV-1 isolates, and its co-crystal structure with the HIV-1 envelope protein gp120 revealed a new loop-based mechanism of CD4-binding-site recognition. Virus and antibody gene sequencing revealed concomitant virus evolution and antibody maturation. Notably, the unmutated common ancestor of the CH103 lineage avidly bound the transmitted/founder HIV-1 envelope glycoprotein, and evolution of antibody neutralization breadth was preceded by extensive viral diversification in and near the CH103 epitope. These data determine the viral and antibody evolution leading to induction of a lineage of HIV-1 broadly neutralizing antibodies, and provide insights into strategies to elicit similar antibodies by vaccination.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3637846/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3637846/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liao, Hua-Xin -- Lynch, Rebecca -- Zhou, Tongqing -- Gao, Feng -- Alam, S Munir -- Boyd, Scott D -- Fire, Andrew Z -- Roskin, Krishna M -- Schramm, Chaim A -- Zhang, Zhenhai -- Zhu, Jiang -- Shapiro, Lawrence -- NISC Comparative Sequencing Program -- Mullikin, James C -- Gnanakaran, S -- Hraber, Peter -- Wiehe, Kevin -- Kelsoe, Garnett -- Yang, Guang -- Xia, Shi-Mao -- Montefiori, David C -- Parks, Robert -- Lloyd, Krissey E -- Scearce, Richard M -- Soderberg, Kelly A -- Cohen, Myron -- Kamanga, Gift -- Louder, Mark K -- Tran, Lillian M -- Chen, Yue -- Cai, Fangping -- Chen, Sheri -- Moquin, Stephanie -- Du, Xiulian -- Joyce, M Gordon -- Srivatsan, Sanjay -- Zhang, Baoshan -- Zheng, Anqi -- Shaw, George M -- Hahn, Beatrice H -- Kepler, Thomas B -- Korber, Bette T M -- Kwong, Peter D -- Mascola, John R -- Haynes, Barton F -- AI067854/AI/NIAID NIH HHS/ -- AI100645/AI/NIAID NIH HHS/ -- P30 AI050410/AI/NIAID NIH HHS/ -- UM1 AI100645/AI/NIAID NIH HHS/ -- Intramural NIH HHS/ -- England -- Nature. 2013 Apr 25;496(7446):469-76. doi: 10.1038/nature12053. Epub 2013 Apr 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Duke University Human Vaccine Institute, Departments of Medicine and Immunology, Duke University School of Medicine, Durham, North Carolina 27710, USA. hliao@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23552890" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/immunology ; Africa ; Amino Acid Sequence ; Antibodies, Monoclonal/chemistry/genetics/immunology ; Antibodies, Neutralizing/*chemistry/genetics/*immunology ; Antigens, CD4/chemistry/immunology ; Cell Lineage ; Cells, Cultured ; Clone Cells/cytology ; Cross Reactions/immunology ; Crystallography, X-Ray ; Epitopes/chemistry/immunology ; *Evolution, Molecular ; HIV Antibodies/*chemistry/genetics/*immunology ; HIV Envelope Protein gp120/chemistry/genetics/immunology/metabolism ; HIV-1/*chemistry/classification/*immunology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neutralization Tests ; Phylogeny ; Protein Structure, Tertiary
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2015-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tong, Yi-Gang -- Shi, Wei-Feng -- Liu, Di -- Qian, Jun -- Liang, Long -- Bo, Xiao-Chen -- Liu, Jun -- Ren, Hong-Guang -- Fan, Hang -- Ni, Ming -- Sun, Yang -- Jin, Yuan -- Teng, Yue -- Li, Zhen -- Kargbo, David -- Dafae, Foday -- Kanu, Alex -- Chen, Cheng-Chao -- Lan, Zhi-Heng -- Jiang, Hui -- Luo, Yang -- Lu, Hui-Jun -- Zhang, Xiao-Guang -- Yang, Fan -- Hu, Yi -- Cao, Yu-Xi -- Deng, Yong-Qiang -- Su, Hao-Xiang -- Sun, Yu -- Liu, Wen-Sen -- Wang, Zhuang -- Wang, Cheng-Yu -- Bu, Zhao-Yang -- Guo, Zhen-Dong -- Zhang, Liu-Bo -- Nie, Wei-Min -- Bai, Chang-Qing -- Sun, Chun-Hua -- An, Xiao-Ping -- Xu, Pei-Song -- Zhang, Xiang-Li-Lan -- Huang, Yong -- Mi, Zhi-Qiang -- Yu, Dong -- Yao, Hong-Wu -- Feng, Yong -- Xia, Zhi-Ping -- Zheng, Xue-Xing -- Yang, Song-Tao -- Lu, Bing -- Jiang, Jia-Fu -- Kargbo, Brima -- He, Fu-Chu -- Gao, George F -- Cao, Wu-Chun -- China Mobile Laboratory Testing Team in Sierra Leone -- England -- Nature. 2015 Oct 22;526(7574):595. doi: 10.1038/nature15255. Epub 2015 Aug 26.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26308898" target="_blank"〉PubMed〈/a〉
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2018-02-27
    Description: Oncolytic virotherapy is an emerging treatment modality that uses replication-competent viruses to destroy cancer cells. M1 is a naturally occurring alphavirus ( Togaviridae ) which shows potent oncolytic activities against many cancers. Accumulation of unfolded proteins during virus replication leads to a transcriptional/translational response known as the unfolded protein response (UPR), which might counteract the antitumor effect of the oncolytic virus. In this report, we show that either pharmacological or biological inhibition of IRE1α or PERK, but not ATF6, substantially increases the oncolytic effects of the M1 virus. Moreover, inhibition of IRE1α blocks M1 virus-induced autophagy, which restricts the antitumor effects of the M1 virus through degradation of viral protein, in glioma cells. In addition, IRE1α suppression significantly increases the oncolytic effect of M1 virus in an orthotopic glioma model. From a molecular pathology study, we found that IRE1α is expressed at lower levels in higher-grade gliomas, suggesting greater antitumor efficacy of the oncolytic virus M1. Taken together, these findings illustrate a defensive mechanism of glioma cells against the oncolytic virus M1 and identify possible approaches to enhance the oncolytic viral protein accumulation and the subsequent lysis of tumor cells. IMPORTANCE Although oncolytic virotherapy is showing great promise in clinical applications, not all patients are benefiting. Identifying inhibitory signals in refractory cancer cells for each oncolytic virus would provide a good chance to increase the therapeutic effect. Here we describe that infection with the oncolytic virus M1 triggers the unfolded protein response (UPR) and subsequent autophagy, while blocking the UPR-autophagy axis significantly potentiates the antitumor efficacy of M1 in vitro and in vivo . A survey of cancer tissue banks revealed that IRE1α, a key element in the UPR pathway, is commonly downregulated in higher-grade human gliomas, suggesting favorable prospects for the application of M1. Our work provides a potential predictor and target for enhancement of the therapeutic effectiveness of the M1 virus. We predict that the mechanism-based combination therapy will promote cancer virotherapy in the future.
    Print ISSN: 0022-538X
    Electronic ISSN: 1098-5514
    Topics: Medicine
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  • 5
    Publication Date: 2013-07-05
    Description: Human infection associated with a novel reassortant avian influenza H7N9 virus has recently been identified in China. A total of 132 confirmed cases and 39 deaths have been reported. Most patients presented with severe pneumonia and acute respiratory distress syndrome. Although the first epidemic has subsided, the presence of a natural reservoir and the disease severity highlight the need to evaluate its risk on human public health and to understand the possible pathogenesis mechanism. Here we show that the emerging H7N9 avian influenza virus poses a potentially high risk to humans. We discover that the H7N9 virus can bind to both avian-type (alpha2,3-linked sialic acid) and human-type (alpha2,6-linked sialic acid) receptors. It can invade epithelial cells in the human lower respiratory tract and type II pneumonocytes in alveoli, and replicated efficiently in ex vivo lung and trachea explant culture and several mammalian cell lines. In acute serum samples of H7N9-infected patients, increased levels of the chemokines and cytokines IP-10, MIG, MIP-1beta, MCP-1, IL-6, IL-8 and IFN-alpha were detected. We note that the human population is naive to the H7N9 virus, and current seasonal vaccination could not provide protection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Jianfang -- Wang, Dayan -- Gao, Rongbao -- Zhao, Baihui -- Song, Jingdong -- Qi, Xian -- Zhang, Yanjun -- Shi, Yonglin -- Yang, Lei -- Zhu, Wenfei -- Bai, Tian -- Qin, Kun -- Lan, Yu -- Zou, Shumei -- Guo, Junfeng -- Dong, Jie -- Dong, Libo -- Zhang, Ye -- Wei, Hejiang -- Li, Xiaodan -- Lu, Jian -- Liu, Liqi -- Zhao, Xiang -- Li, Xiyan -- Huang, Weijuan -- Wen, Leying -- Bo, Hong -- Xin, Li -- Chen, Yongkun -- Xu, Cuilin -- Pei, Yuquan -- Yang, Yue -- Zhang, Xiaodong -- Wang, Shiwen -- Feng, Zijian -- Han, Jun -- Yang, Weizhong -- Gao, George F -- Wu, Guizhen -- Li, Dexin -- Wang, Yu -- Shu, Yuelong -- England -- Nature. 2013 Jul 25;499(7459):500-3. doi: 10.1038/nature12379. Epub 2013 Jul 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute for Viral Disease Control and Prevention, China CDC, Key Laboratory for Medical Virology, National Health and Family Planning Commission, Beijing 102206, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23823727" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/immunology ; Birds/virology ; Bronchi/cytology/metabolism/virology ; Cell Line ; Chemokines/blood ; China ; Cross Reactions/immunology ; Epithelial Cells/virology ; Host Specificity ; Humans ; In Vitro Techniques ; Influenza A Virus, H5N1 Subtype/immunology/physiology ; Influenza A virus/immunology/pathogenicity/*physiology ; Influenza Vaccines/immunology ; Influenza in Birds/transmission/*virology ; Influenza, Human/blood/immunology/virology ; Lung/virology ; N-Acetylneuraminic Acid/analogs & derivatives/chemistry/metabolism ; Organ Specificity ; Pulmonary Alveoli/cytology/metabolism/virology ; Receptors, Virus/chemistry/*metabolism ; Trachea/virology ; Virus Replication ; Zoonoses/transmission/virology
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2015-05-15
    Description: A novel Ebola virus (EBOV) first identified in March 2014 has infected more than 25,000 people in West Africa, resulting in more than 10,000 deaths. Preliminary analyses of genome sequences of 81 EBOV collected from March to June 2014 from Guinea and Sierra Leone suggest that the 2014 EBOV originated from an independent transmission event from its natural reservoir followed by sustained human-to-human infections. It has been reported that the EBOV genome variation might have an effect on the efficacy of sequence-based virus detection and candidate therapeutics. However, only limited viral information has been available since July 2014, when the outbreak entered a rapid growth phase. Here we describe 175 full-length EBOV genome sequences from five severely stricken districts in Sierra Leone from 28 September to 11 November 2014. We found that the 2014 EBOV has become more phylogenetically and genetically diverse from July to November 2014, characterized by the emergence of multiple novel lineages. The substitution rate for the 2014 EBOV was estimated to be 1.23 x 10(-3) substitutions per site per year (95% highest posterior density interval, 1.04 x 10(-3) to 1.41 x 10(-3) substitutions per site per year), approximating to that observed between previous EBOV outbreaks. The sharp increase in genetic diversity of the 2014 EBOV warrants extensive EBOV surveillance in Sierra Leone, Guinea and Liberia to better understand the viral evolution and transmission dynamics of the ongoing outbreak. These data will facilitate the international efforts to develop vaccines and therapeutics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tong, Yi-Gang -- Shi, Wei-Feng -- Liu, Di -- Qian, Jun -- Liang, Long -- Bo, Xiao-Chen -- Liu, Jun -- Ren, Hong-Guang -- Fan, Hang -- Ni, Ming -- Sun, Yang -- Jin, Yuan -- Teng, Yue -- Li, Zhen -- Kargbo, David -- Dafae, Foday -- Kanu, Alex -- Chen, Cheng-Chao -- Lan, Zhi-Heng -- Jiang, Hui -- Luo, Yang -- Lu, Hui-Jun -- Zhang, Xiao-Guang -- Yang, Fan -- Hu, Yi -- Cao, Yu-Xi -- Deng, Yong-Qiang -- Su, Hao-Xiang -- Sun, Yu -- Liu, Wen-Sen -- Wang, Zhuang -- Wang, Cheng-Yu -- Bu, Zhao-Yang -- Guo, Zhen-Dong -- Zhang, Liu-Bo -- Nie, Wei-Min -- Bai, Chang-Qing -- Sun, Chun-Hua -- An, Xiao-Ping -- Xu, Pei-Song -- Zhang, Xiang-Li-Lan -- Huang, Yong -- Mi, Zhi-Qiang -- Yu, Dong -- Yao, Hong-Wu -- Feng, Yong -- Xia, Zhi-Ping -- Zheng, Xue-Xing -- Yang, Song-Tao -- Lu, Bing -- Jiang, Jia-Fu -- Kargbo, Brima -- He, Fu-Chu -- Gao, George F -- Cao, Wu-Chun -- China Mobile Laboratory Testing Team in Sierra Leone -- England -- Nature. 2015 Aug 6;524(7563):93-6. doi: 10.1038/nature14490. Epub 2015 May 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉State Key Laboratory of Pathogen and Biosecurity, Beijing 100071, China. ; Institute of Pathogen Biology, Taishan Medical College, Taian 271000, China. ; Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China. ; Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun 130122, China. ; Beijing Key Laboratory of New Molecular Diagnostics Technology, Beijing 100850, China. ; Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 102206, China. ; Sierra Leone Ministry of Health and Sanitation, Freetown, Sierra Leone. ; Sierra Leone-China Friendship Hospital, Freetown, Sierra Leone. ; BGI-Shenzhen, Shenzhen 518083, China. ; Wellcome Trust Sanger Institute, Cambridge CB10 1SA, UK. ; Chinese Academy of Medical Sciences &Peking Union Medical College, Beijing 100730, China. ; Institute of Environmental Health and Related Product Safety, Chinese Center for Disease Control and Prevention, Beijing 100021, China. ; The No. 302 Hospital, Beijing 100039, China. ; The No. 307 Hospital, Beijing 100071, China. ; Department of international cooperation, National Health and Family Planning Commission, Beijing 100044, China. ; State Key Laboratory of Proteomics, Beijing 102206, China. ; 1] Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China [2] Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 102206, China [3] Chinese Center for Disease Control and Prevention, Beijing 102206, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25970247" target="_blank"〉PubMed〈/a〉
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 43 (1987), S. 754-756 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 43 (1987), S. 2130-2132 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 47 (1991), S. 459-461 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 10
    Publication Date: 2018-08-01
    Description: Porcine hemagglutinating encephalomyelitis virus (PHEV) is a highly neurovirulent coronavirus and causes neurological dysfunction in the central nervous system (CNS), but the neuropathological mechanism of PHEV remains poorly understood. We report that Unc51-like kinase 1 (Ulk1/Unc51.1) is a pivotal regulator of PHEV-induced neurological disorders and functions to selectively control the initiation of nerve growth factor (NGF)/TrkA endosome trafficking. We first identified the function of Ulk1 by histopathologic evaluation in a PHEV-infected mouse model in which neuronal loss was accompanied by the suppression of Ulk1 expression. Morphogenesis assessments in the primary cortical neurons revealed that overexpression or mutations of Ulk1 modulated neurite outgrowth, collateral sprouting, and endosomal transport. Likewise, Ulk1 expression was decreased following PHEV infection, suggesting that there was a correlation between the neurodegeneration and functional Ulk1 deficiency. We then showed that Ulk1 forms a multiprotein complex with TrkA and the early endosome marker Rab5 and that Ulk1 defects lead to either blocking of NGF/TrkA endocytosis or premature degradation of pTrkA via constitutive activation of the Rab5 GTPase. Further investigation determined that the ectopic expression of Rab5 mutants induces aberrant endosomal accumulation of activated pTrkA, proving that targeting of Ulk1-TrkA-NGF signaling to the retrograde transport route in the neurodegenerative process that underlies PHEV infection is dependent on Rab5 GTPase activity. Therefore, we described a long-distance signaling mechanism of PHEV-driven deficits in neurons and suggested that such Ulk1 repression may result in limited NGF/TrkA retrograde signaling within activated Rab5 endosomes, explaining the progressive failure of neurite outgrowth and survival. IMPORTANCE Porcine hemagglutinating encephalomyelitis virus (PHEV) is a neurotropic coronavirus and targets neurons in the nervous system for proliferation, frequently leaving behind grievous neurodegeneration. Structural plasticity disorders occur in the axons, dendrites, and dendritic spines of PHEV-infected neurons, and dysfunction of this neural process may contribute to neurologic pathologies, but the mechanisms remain undetermined. Further understanding of the neurological manifestations underlying PHEV infection in the CNS may provide insights into both neurodevelopmental and neurodegenerative diseases that may be conducive to targeted approaches for treatment. The significance of our research is in identifying an Ulk1-related neurodegenerative mechanism, focusing on the regulatory functions of Ulk1 in the transport of long-distance trophic signaling endosomes, thereby explaining the progressive failure of neurite outgrowth and survival associated with PHEV aggression. This is the first report to define a mechanistic link between alterations in signaling from endocytic pathways and the neuropathogenesis of PHEV-induced CNS disease.
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    Topics: Medicine
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