Papain-Like Protease Regulates SARS-Cov-2 Viral Spread and Innate Immunity
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Genetic Variations of the Bovine MX1 and Their Association with Mastitis
Czech J. Anim. Sci., 62, 2017 (4): 157–167 Original Paper doi: 10.17221/97/2015-CJAS Genetic Variations of the Bovine MX1 and Their Association with Mastitis Ningbo Chen, Fengqiao Wang, Nongqi Yu, Yuan Gao, Jieping Huang, Yongzhen Huang, Xianyon Lan, Chuzhao Lei, Hong Chen, Ruihua Dang* College of Animal Science and Technology, Northwest A&F University, Yangling, P.R. China *Corresponding author: [email protected] ABSTRACT Chen N., Wang F., Yu N., Gao Y., Huang J., Huang Y., Lan X., Lei C., Chen H., Dang R. (2017): Genetic variations of the bovine MX1 and their association with mastitis. Czech J. Anim. Sci., 62, 157–167. The primary agent of mastitis is a wide spectrum of bacterial strains; however, viral-related mastitis has also been reported. The MX dynamin-like GTPase 1 (MX1) gene has been demonstrated to confer positive antiviral responses to many viruses, and may be a suitable candidate gene for the study of disease resistance in dairy cattle. The present study was conducted to investigate the genetic diversity of theMX1 gene in Chinese cattle breeds and its effects on mastitis in Holstein cows. First, polymorphisms were identified in the complete coding region of the bovine MX1 gene in 14 Chinese cattle breeds. An association study was then carried out, utilizing polymorphisms detected in Holstein cows to determine the associations of these single nucleotide polymor- phisms (SNPs) with mastitis. We identified 13 previously reported SNPs in Chinese domestic cattle and four of them in Holstein cattle. A novel 12 bp indel was also discovered in Holstein cattle. -
Copy Number Variation and Huntington's Disease
UNIVERSIDADE DE LISBOA FACULDADE DE MEDICINA DE LISBOA Copy number variation and Huntington’s disease Angelica Vittori Ramo das Ciências Biomédicas Especialidade – Neurociências Outubro 2013 UNIVERSIDADE DE LISBOA FACULDADE DE MEDICINA DE LISBOA Copy number variation and Huntington’s disease Candidata: Angelica Vittori Orientadores: Prof . Doutor Tiago Fleming Outeiro Doutor Flaviano Giorgini Doutor Edward J. Hollox Ramo das Ciências Biomédicas Especialidade – Neurociências Todas as afirmações efectuadas no presente documento são da exclusiva II responsabilidade do seu autor, não cabendo qualquer responsabilidade à faculdade de medicina de lisboa pelos conteúdos nela apresentados. A impressão são da exclusiva está dissertação foi aprovada pelo Conselho Cientifico da Faculdade de Medicina em reunião de 19 de Novembro de 2013. III Resumo A variação de número de cópias (CNV em inglês) é uma modificação de uma sequência de DNA que apresenta uma inserção ou deleção em comparação com um genoma de referência com um número de cópias de N = 2. Com um comprimento variável, desde 50 pares de bases até várias megabases, as CNVs identificadas têm um tamanho médio de ~ 3 Kb e representam cerca de 4% do genoma humano. As CNVs, como outras variações genéticas, podem afetar directamente os níveis de expressão dos genes afectados. Os efeitos indirectos na expressão genética podem ser causados por alterações da posição, interrompendo o quadro de leitura do gene ou posteriormente, perturbando as redes de regulação genética. Foi demonstrado que as CNVs são em grande parte responsáveis pela evolução humana e diversidade genética entre os indivíduos. A relevância das CNVs no genoma humano foi salientada por vários estudos de associação que mostraram o efeito das CNVs na susceptibilidade a doenças neurodegenerativas, doenças de características complexas, e por serem a principal causa do aparecimento de doenças mendelianas ou por conferirem um fenótipo benigno. -
Interferon-Λ Enhances Adaptive Mucosal Immunity by Boosting Release of Thymic Stromal Lymphopoietin
ARTICLES https://doi.org/10.1038/s41590-019-0345-x Interferon-λ enhances adaptive mucosal immunity by boosting release of thymic stromal lymphopoietin Liang Ye1, Daniel Schnepf1,2, Jan Becker1, Karolina Ebert3, Yakup Tanriver3,4,5, Valentina Bernasconi 6, Hans Henrik Gad7, Rune Hartmann 7, Nils Lycke6 and Peter Staeheli 1,4* Interferon-λ (IFN-λ) acts on mucosal epithelial cells and thereby confers direct antiviral protection. In contrast, the role of IFN-λ in adaptive immunity is far less clear. Here, we report that mice deficient in IFN-λ signaling exhibited impaired CD8+ T cell and antibody responses after infection with a live-attenuated influenza virus. Virus-induced release of IFN-λ triggered the synthesis of thymic stromal lymphopoietin (TSLP) by M cells in the upper airways that, in turn, stimulated migratory dendritic cells and boosted antigen-dependent germinal center reactions in draining lymph nodes. The IFN-λ–TSLP axis also boosted pro- duction of the immunoglobulins IgG1 and IgA after intranasal immunization with influenza virus subunit vaccines and improved survival of mice after challenge with virulent influenza viruses. IFN-λ did not influence the efficacy of vaccines applied by sub- cutaneous or intraperitoneal routes, indicating that IFN-λ plays a vital role in potentiating adaptive immune responses that initiate at mucosal surfaces. nterferon-λ (IFN-λ) is an antiviral cytokine produced in response M cells which, in turn, influences germinal center responses by act- to viral infection in a variety of cell types, including airway epithe- ing on migratory dendritic cells (DCs). This previously unknown Ilial cells1,2. -
The 125Th Lys and 145Th Thr Amino Acids in the Gtpase Domain of Goose Mx Confer Its Antiviral Activity Against the Tembusu Virus
viruses Article The 125th Lys and 145th Thr Amino Acids in the GTPase Domain of Goose Mx Confer Its Antiviral Activity against the Tembusu Virus Shun Chen 1,2,3,*,†, Miao Zeng 1,†, Peng Liu 1, Chao Yang 1, Mingshu Wang 1,2,3, Renyong Jia 1,2,3, Dekang Zhu 2,3 ID , Mafeng Liu 1,2,3, Qiao Yang 1,2,3, Ying Wu 1,2,3, Xinxin Zhao 1,2,3 and Anchun Cheng 1,2,3,* ID 1 Institute of Preventive Veterinary Medicine, Sichuan Agricultural University, No. 211 Huimin Road, Wenjiang District, Chengdu 611130, Sichuan, China; [email protected] (M.Z.); [email protected] (P.L.); [email protected] (C.Y.); [email protected] (M.W.); [email protected] (R.J.); [email protected] (M.L.); [email protected] (Q.Y.); [email protected] (Y.W.); [email protected] (X.Z.) 2 Research Center of Avian Disease, College of Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, Sichuan, China; [email protected] 3 Key Laboratory of Animal Disease and Human Health of Sichuan Province, Sichuan Agricultural University, Chengdu 611130, Sichuan, China * Correspondence: [email protected] (S.C.); [email protected] (A.C.); Tel.: +86-028-8629-1482 (S.C.) † These authors contributed equally as co-first authors of this work. Received: 7 June 2018; Accepted: 4 July 2018; Published: 6 July 2018 Abstract: The Tembusu virus (TMUV) is an avian pathogenic flavivirus that causes a highly contagious disease and catastrophic losses to the poultry industry. The myxovirus resistance protein (Mx) of innate immune effectors is a key antiviral “workhorse” of the interferon (IFN) system. -
Microarray Analysis of Novel Genes Involved in HSV- 2 Infection
Microarray analysis of novel genes involved in HSV- 2 infection Hao Zhang Nanjing University of Chinese Medicine Tao Liu ( [email protected] ) Nanjing University of Chinese Medicine https://orcid.org/0000-0002-7654-2995 Research Article Keywords: HSV-2 infection,Microarray analysis,Histospecic gene expression Posted Date: May 12th, 2021 DOI: https://doi.org/10.21203/rs.3.rs-517057/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/19 Abstract Background: Herpes simplex virus type 2 infects the body and becomes an incurable and recurring disease. The pathogenesis of HSV-2 infection is not completely clear. Methods: We analyze the GSE18527 dataset in the GEO database in this paper to obtain distinctively displayed genes(DDGs)in the total sequential RNA of the biopsies of normal and lesioned skin groups, healed skin and lesioned skin groups of genital herpes patients, respectively.The related data of 3 cases of normal skin group, 4 cases of lesioned group and 6 cases of healed group were analyzed.The histospecic gene analysis , functional enrichment and protein interaction network analysis of the differential genes were also performed, and the critical components were selected. Results: 40 up-regulated genes and 43 down-regulated genes were isolated by differential performance assay. Histospecic gene analysis of DDGs suggested that the most abundant system for gene expression was the skin, immune system and the nervous system.Through the construction of core gene combinations, protein interaction network analysis and selection of histospecic distribution genes, 17 associated genes were selected CXCL10,MX1,ISG15,IFIT1,IFIT3,IFIT2,OASL,ISG20,RSAD2,GBP1,IFI44L,DDX58,USP18,CXCL11,GBP5,GBP4 and CXCL9.The above genes are mainly located in the skin, immune system, nervous system and reproductive system. -
Type III Interferons Disrupt the Lung Epithelial Barrier Upon Viral Recognition
bioRxiv preprint doi: https://doi.org/10.1101/2020.05.05.077867; this version posted May 5, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 1 Type III interferons disrupt the lung epithelial barrier upon viral recognition. 2 3 Achille Broggi1,*, Sreya Ghosh1,*, Benedetta Sposito1,2,*, Roberto Spreafico3, Fabio Balzarini1,2, 4 Antonino Lo Cascio1,2, Nicola Clementi4, Maria De Santis5, Nicasio Mancini4,6, Francesca 5 Granucci2,7, Ivan Zanoni1,2,8,#. 6 7 8 1 Harvard Medical School, Boston Children’s Hospital, Division of Immunology, Boston, United 9 States. 10 2 Department of Biotechnology and Biosciences, University of Milano - Bicocca, Milan, Italy. 11 3 Institute for Quantitative and Computational Biosciences, University of California, Los Angeles, 12 United States. 13 4 Laboratory of Medical Microbiology and Virology, Vita-Salute San Raffaele University, Milan, 14 Italy. 15 5 Rheumatology and Clinical Immunology, Humanitas Clinical and Research Center - IRCCS, 16 Rozzano, Italy. 17 6 IRCCS San Raffaele Hospital, Milan, Italy. 18 7 INGM-National Institute of Molecular Genetics "Romeo ed Enrica Invernizzi" Milan, Italy. 19 8 Harvard Medical School, Boston Children’s Hospital, Division of Gastroenterology, Boston, 20 United States. 21 * Equal contribution 22 # Corresponding author: [email protected] 23 24 25 26 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.05.05.077867; this version posted May 5, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. -
Alpha Defensin 1 Antibody / DEFA1 (R32739)
Alpha Defensin 1 Antibody / DEFA1 (R32739) Catalog No. Formulation Size R32739 0.5mg/ml if reconstituted with 0.2ml sterile DI water 100 ug Bulk quote request Availability 1-3 business days Species Reactivity Human, Rat Format Antigen affinity purified Clonality Polyclonal (rabbit origin) Isotype Rabbit IgG Purity Antigen affinity Buffer Lyophilized from 1X PBS with 2.5% BSA, 0.025% sodium azide UniProt P59665 Applications Western Blot : 0.5-1ug/ml Limitations This Alpha Defensin 1 antibody is available for research use only. Western blot testing of 1) rat testis and 2) human HeLa lysate with Alpha Defensin 1 antibody at 0.5ug/ml. Predicted molecular weight ~10 kDa. Description Defensin, alpha 1, also known as human alpha defensin 1, human neutrophil peptide 1 (HNP-1) or neutrophil defensin 1 is a human protein that is encoded by the DEFA1 gene. Defensins are a family of antimicrobial and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. The protein encoded by this gene, defensin, alpha 1, is found in the microbicidal granules of neutrophils and likely plays a role in phagocyte-mediated host defense. Several alpha defensin genes are clustered on chromosome 8. This gene differs from defensin, alpha 3 by only one amino acid. This gene and the gene encoding defensin, alpha 3 are both subject to copy number variation. -
DEFA1 Rabbit Pab
Leader in Biomolecular Solutions for Life Science DEFA1 Rabbit pAb Catalog No.: A6897 Basic Information Background Catalog No. Defensins are a family of antimicrobial and cytotoxic peptides thought to be involved in host A6897 defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Observed MW Members of the defensin family are highly similar in protein sequence and distinguished by a 10KDa conserved cysteine motif. The protein encoded by this gene, defensin, alpha 1, is found in the microbicidal granules of neutrophils and likely plays a role in phagocyte-mediated host defense. Several alpha defensin genes are clustered on chromosome 8. This gene differs Calculated MW from defensin, alpha 3 by only one amino acid. This gene and the gene encoding defensin, 10kDa alpha 3 are both subject to copy number variation. Category Primary antibody Applications WB, IHC, IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 1667 P59665 IHC 1:50 - 1:100 Immunogen IF 1:50 - 1:100 Recombinant fusion protein containing a sequence corresponding to amino acids 1-94 of human DEFA1 (NP_004075.1). Synonyms DEFA1;DEF1;DEFA2;HNP-1;HP-1;HP1;MRS Contact Product Information 400-999-6126 Source Isotype Purification Rabbit IgG Affinity purification [email protected] Storage www.abclonal.com.cn Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using DEFA1 antibody (A6897) at 1:1000 dilution. -
Additive Loss-Of-Function Proteasome Subunit Mutations in CANDLE/PRAAS Patients Promote Type I IFN Production
Amendment history: Erratum (February 2016) Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS patients promote type I IFN production Anja Brehm, … , Ivona Aksentijevich, Raphaela Goldbach-Mansky J Clin Invest. 2015;125(11):4196-4211. https://doi.org/10.1172/JCI81260. Research Article Immunology Autosomal recessive mutations in proteasome subunit β 8 (PSMB8), which encodes the inducible proteasome subunit β5i, cause the immune-dysregulatory disease chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature (CANDLE), which is classified as a proteasome-associated autoinflammatory syndrome (PRAAS). Here, we identified 8 mutations in 4 proteasome genes, PSMA3 (encodes α7), PSMB4 (encodes β7), PSMB9 (encodes β1i), and proteasome maturation protein (POMP), that have not been previously associated with disease and 1 mutation inP SMB8 that has not been previously reported. One patient was compound heterozygous for PSMB4 mutations, 6 patients from 4 families were heterozygous for a missense mutation in 1 inducible proteasome subunit and a mutation in a constitutive proteasome subunit, and 1 patient was heterozygous for a POMP mutation, thus establishing a digenic and autosomal dominant inheritance pattern of PRAAS. Function evaluation revealed that these mutations variably affect transcription, protein expression, protein folding, proteasome assembly, and, ultimately, proteasome activity. Moreover, defects in proteasome formation and function were recapitulated by siRNA-mediated knockdown of the respective -
The Genetic Architecture of Down Syndrome Phenotypes Revealed by High-Resolution Analysis of Human Segmental Trisomies
The genetic architecture of Down syndrome phenotypes revealed by high-resolution analysis of human segmental trisomies Jan O. Korbela,b,c,1, Tal Tirosh-Wagnerd,1, Alexander Eckehart Urbane,f,1, Xiao-Ning Chend, Maya Kasowskie, Li Daid, Fabian Grubertf, Chandra Erdmang, Michael C. Gaod, Ken Langeh,i, Eric M. Sobelh, Gillian M. Barlowd, Arthur S. Aylsworthj,k, Nancy J. Carpenterl, Robin Dawn Clarkm, Monika Y. Cohenn, Eric Dorano, Tzipora Falik-Zaccaip, Susan O. Lewinq, Ira T. Lotto, Barbara C. McGillivrayr, John B. Moeschlers, Mark J. Pettenatit, Siegfried M. Pueschelu, Kathleen W. Raoj,k,v, Lisa G. Shafferw, Mordechai Shohatx, Alexander J. Van Ripery, Dorothy Warburtonz,aa, Sherman Weissmanf, Mark B. Gersteina, Michael Snydera,e,2, and Julie R. Korenbergd,h,bb,2 Departments of aMolecular Biophysics and Biochemistry, eMolecular, Cellular, and Developmental Biology, and fGenetics, Yale University School of Medicine, New Haven, CT 06520; bEuropean Molecular Biology Laboratory, 69117 Heidelberg, Germany; cEuropean Molecular Biology Laboratory (EMBL) Outstation Hinxton, EMBL-European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA, United Kingdom; dMedical Genetics Institute, Cedars–Sinai Medical Center, Los Angeles, CA 90048; gDepartment of Statistics, Yale University, New Haven, CT 06520; Departments of hHuman Genetics, and iBiomathematics, University of California, Los Angeles, CA 90095; Departments of jPediatrics and kGenetics, University of North Carolina, Chapel Hill, NC 27599; lCenter for Genetic Testing, -
Cardiac SARS‐Cov‐2 Infection Is Associated with Distinct Tran‐ Scriptomic Changes Within the Heart
Cardiac SARS‐CoV‐2 infection is associated with distinct tran‐ scriptomic changes within the heart Diana Lindner, PhD*1,2, Hanna Bräuninger, MS*1,2, Bastian Stoffers, MS1,2, Antonia Fitzek, MD3, Kira Meißner3, Ganna Aleshcheva, PhD4, Michaela Schweizer, PhD5, Jessica Weimann, MS1, Björn Rotter, PhD9, Svenja Warnke, BSc1, Carolin Edler, MD3, Fabian Braun, MD8, Kevin Roedl, MD10, Katharina Scher‐ schel, PhD1,12,13, Felicitas Escher, MD4,6,7, Stefan Kluge, MD10, Tobias B. Huber, MD8, Benjamin Ondruschka, MD3, Heinz‐Peter‐Schultheiss, MD4, Paulus Kirchhof, MD1,2,11, Stefan Blankenberg, MD1,2, Klaus Püschel, MD3, Dirk Westermann, MD1,2 1 Department of Cardiology, University Heart and Vascular Center Hamburg, Germany. 2 DZHK (German Center for Cardiovascular Research), partner site Hamburg/Kiel/Lübeck. 3 Institute of Legal Medicine, University Medical Center Hamburg‐Eppendorf, Germany. 4 Institute for Cardiac Diagnostics and Therapy, Berlin, Germany. 5 Department of Electron Microscopy, Center for Molecular Neurobiology, University Medical Center Hamburg‐Eppendorf, Germany. 6 Department of Cardiology, Charité‐Universitaetsmedizin, Berlin, Germany. 7 DZHK (German Centre for Cardiovascular Research), partner site Berlin, Germany. 8 III. Department of Medicine, University Medical Center Hamburg‐Eppendorf, Germany. 9 GenXPro GmbH, Frankfurter Innovationszentrum, Biotechnologie (FIZ), Frankfurt am Main, Germany. 10 Department of Intensive Care Medicine, University Medical Center Hamburg‐Eppendorf, Germany. 11 Institute of Cardiovascular Sciences, -
DEFA1) Antibody Catalogue No.:Abx005247
Datasheet Version: 1.0.0 Revision date: 19 Nov 2020 Defensin Alpha 1, Neutrophil (DEFA1) Antibody Catalogue No.:abx005247 Western blot analysis of extracts of various cell lines, using DEFA1 antibody (abx005247) at 1/1000 dilution. Immunohistochemistry of paraffin-embedded rat heart using DEFA1 antibody (abx005247) at dilution of 1/100 (40x lens). Immunofluorescence analysis of HeLa cells using DEFA1 antibody (abx005247). Blue: DAPI for nuclear staining. DEFA1 Antibody is a Rabbit Polyclonal antibody against DEFA1. Defensins are a family of antimicrobial and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. The protein encoded by this gene, defensin, alpha 1, is found in the microbicidal granules of neutrophils and likely plays a role in phagocyte-mediated host defense. Several alpha defensin genesFor are clustered on chromosomeReference 8. This gene differs from defensin, alpha Only 3 by only one amino acid. This gene and the gene encoding defensin, alpha 3 are both subject to copy number variation. Target: DEFA1 Clonality: Polyclonal Reactivity: Human, Mouse, Rat v1.0.0 Abbexa Ltd, Cambridge, UK · Phone: +44 1223 755950 · Fax: +44 1223 755951 1 Abbexa LLC, Houston, TX, USA · Phone: +1 832 327 7413 www.abbexa.com · Email: [email protected] Datasheet Version: 1.0.0 Revision date: 19 Nov 2020 Tested Applications: WB, IHC, IF/ICC Host: Rabbit Recommended dilutions: WB: 1/500 - 1/2000, IHC: 1/50 - 1/100, IF/ICC: 1/50 - 1/100.