المؤلفون: Jacob D. Negrey, Rachna B. Reddy, Erik J. Scully, Sarah Phillips-Garcia, Leah A. Owens, Kevin E. Langergraber, John C. Mitani, Melissa Emery Thompson, Richard W. Wrangham, Martin N. Muller, Emily Otali, Zarin Machanda, David Hyeroba, Kristine A. Grindle, Tressa E. Pappas, Ann C. Palmenberg, James E. Gern, Tony L. Goldberg

المصدر: Emerging Microbes and Infections, Vol 8, Iss 1, Pp 139-149 (2019)

مصطلحات موضوعية: Pneumoviridae, Metapneumovirus, Paramyxoviridae, Respirovirus, Human respirovirus 3, Parainfluenza virus 3, Infectious and parasitic diseases, RC109-216, Microbiology, QR1-502

الوصف: ABSTRACTRespiratory viruses of human origin infect wild apes across Africa, sometimes lethally. Here we report simultaneous outbreaks of two distinct human respiratory viruses, human metapneumovirus (MPV; Pneumoviridae: Metapneumovirus) and human respirovirus 3 (HRV3; Paramyxoviridae; Respirovirus, formerly known as parainfluenza virus 3), in two chimpanzee (Pan troglodytes schweinfurthii) communities in the same forest in Uganda in December 2016 and January 2017. The viruses were absent before the outbreaks, but each was present in ill chimpanzees from one community during the outbreak period. Clinical signs and gross pathologic changes in affected chimpanzees closely mirrored symptoms and pathology commonly observed in humans for each virus. Epidemiologic modelling showed that MPV and HRV3 were similarly transmissible (R0 of 1.27 and 1.48, respectively), but MPV caused 12.2% mortality mainly in infants and older chimpanzees, whereas HRV3 caused no direct mortality. These results are consistent with the higher virulence of MPV than HRV3 in humans, although both MPV and HRV3 cause a significant global disease burden. Both viruses clustered phylogenetically within groups of known human variants, with MPV closely related to a lethal 2009 variant from mountain gorillas (Gorilla beringei beringei), suggesting two independent and simultaneous reverse zoonotic origins, either directly from humans or via intermediary hosts. These findings expand our knowledge of human origin viruses threatening wild chimpanzees and suggest that such viruses might be differentiated by their comparative epidemiological dynamics and pathogenicity in wild apes. Our results also caution against assuming common causation in coincident outbreaks.

وصف الملف: electronic resource

العلاقة: https://doaj.org/toc/2222-1751Test

الوصول الحر: https://doaj.org/article/97e317b4d7ed4c8aa55420e3de0ce8abTest

المؤلفون: Erik J. Scully, Sarmi Basnet, Richard W. Wrangham, Martin N. Muller, Emily Otali, David Hyeroba, Kristine A. Grindle, Tressa E. Pappas, Melissa Emery Thompson, Zarin Machanda, Kelly E. Watters, Ann C. Palmenberg, James E. Gern, Tony L. Goldberg

المصدر: Emerging Infectious Diseases, Vol 24, Iss 2, Pp 267-274 (2018)

مصطلحات موضوعية: Picornaviridae, enterovirus, rhinovirus, rhinovirus C, chimpanzee, Uganda, Medicine, Infectious and parasitic diseases, RC109-216

الوصف: We describe a lethal respiratory outbreak among wild chimpanzees in Uganda in 2013 for which molecular and epidemiologic analyses implicate human rhinovirus C as the cause. Postmortem samples from an infant chimpanzee yielded near-complete genome sequences throughout the respiratory tract; other pathogens were absent. Epidemiologic modeling estimated the basic reproductive number (R0) for the epidemic as 1.83, consistent with the common cold in humans. Genotyping of 41 chimpanzees and examination of 24 published chimpanzee genomes from subspecies across Africa showed universal homozygosity for the cadherin-related family member 3 CDHR3-Y529 allele, which increases risk for rhinovirus C infection and asthma in human children. These results indicate that chimpanzees exhibit a species-wide genetic susceptibility to rhinovirus C and that this virus, heretofore considered a uniquely human pathogen, can cross primate species barriers and threatens wild apes. We advocate engineering interventions and prevention strategies for rhinovirus infections for both humans and wild apes.

وصف الملف: electronic resource

العلاقة: https://wwwnc.cdc.gov/eid/article/24/2/17-0778_articleTest; https://doaj.org/toc/1080-6040Test; https://doaj.org/toc/1080-6059Test

الوصول الحر: https://doaj.org/article/d5ea4c58ab394031afd1ca8f9c60714eTest

المؤلفون: Theodor F. Griggs, Yury A. Bochkov, Sarmila Basnet, Thomas R. Pasic, Rebecca A. Brockman-Schneider, Ann C. Palmenberg, James E. Gern

المصدر: Respiratory Research, Vol 18, Iss 1, Pp 1-11 (2017)

مصطلحات موضوعية: Rhinovirus C, Air-liquid interface, Ciliated cells, CDHR3, Bronchial epithelium, Diseases of the respiratory system, RC705-779

الوصف: Abstract Background The Rhinovirus C (RV-C), first identified in 2006, produce high symptom burdens in children and asthmatics, however, their primary target host cell in the airways remains unknown. Our primary hypotheses were that RV-C target ciliated airway epithelial cells (AECs), and that cell specificity is determined by restricted and high expression of the only known RV-C cell-entry factor, cadherin related family member 3 (CDHR3). Methods RV-C15 (C15) infection in differentiated human bronchial epithelial cell (HBEC) cultures was assessed using immunofluorescent and time-lapse epifluorescent imaging. Morphology of C15-infected differentiated AECs was assessed by immunohistochemistry. Results C15 produced a scattered pattern of infection, and infected cells were shed from the epithelium. The percentage of cells infected with C15 varied from 1.4 to 14.7% depending on cell culture conditions. Infected cells had increased staining for markers of ciliated cells (acetylated-alpha-tubulin [aat], p

وصف الملف: electronic resource

العلاقة: http://link.springer.com/article/10.1186/s12931-017-0567-0Test; https://doaj.org/toc/1465-993XTest

الوصول الحر: https://doaj.org/article/93106c2d94fc4ee6ad472ec327b259c6Test

المؤلفون: Woonghee Lee, Ronnie O. Frederick, Marco Tonelli, Ann C. Palmenberg

المصدر: Viruses, Vol 13, Iss 2, p 159 (2021)

مصطلحات موضوعية: rhinovirus C, receptor, CDHR3, NMR structure, Microbiology, QR1-502

الوصف: Cadherin Related Family Member 3 (CDHR3) is the identified and required cellular receptor for all virus isolates in the rhinovirus-C species (RV-C). Cryo-EM determinations recently resolved the atomic structure of RV-C15a, and subsequently, a complex of this virus bound to CDHR3 extracellular domain 1 (EC1), the N-terminal portion of this receptor responsible for virus interactions. The EC1 binds to a hypervariable sequence footprint on the virus surface, near the 3-fold axis of icosahedral symmetry. The key contacts involve discontinuous residues from 3 viral proteins, VP1, VP2 and VP3. That single cryo-EM EC1 structure, however, could not resolve whether the virus-receptor interface was structurally adaptable to accommodate multiple virus sequences. We now report the solution NMR determination of CDHR3 EC1, showing that this protein, in fact, is mostly inflexible, particularly in the virus-binding face. The new, higher resolution dataset identifies 3 cis-Pro residues in important loop regions, where they can influence both rigidity and overall protein conformation. The data also provide clarification about the residues involved in essential calcium ion binding, and a potential CDHR3 surface groove feature that may be involved in native protein interactions with cellular partners.

وصف الملف: electronic resource

العلاقة: https://www.mdpi.com/1999-4915/13/2/159Test; https://doaj.org/toc/1999-4915Test

الوصول الحر: https://doaj.org/article/8431a586fa374a849275d2de1f61e327Test

المؤلفون: Anna S. Heffron (6013853), Sean J. McIlwain (3221448), Maya F. Amjadi (10994525), David A. Baker (7494542), Saniya Khullar (10994528), Tammy Armbrust (7115156), Peter J. Halfmann (7115153), Yoshihiro Kawaoka (18302), Ajay K. Sethi (10994531), Ann C. Palmenberg (10994534), Miriam A. Shelef (5703491), David H. O’Connor (6639923), Irene M. Ong (8353449)

مصطلحات موضوعية: Biophysics, Biochemistry, Microbiology, Molecular Biology, Biotechnology, Evolutionary Biology, Immunology, Infectious Diseases, Virology, Computational Biology, Biological Sciences not elsewhere classified, Information Systems not elsewhere classified, peptide sequences, CoV proteins, syndrome coronavirus 2, SARS-CoV -2, SARS-CoV -2 infection bind, use ultradense peptide microarray m., SARS-CoV -2 infection, reactive B cell epitopes, Illness severity, enzyme-linked immunosorbent assay, Coronavirus membrane, humoral immunogens, ELISA, antibody responses, map 79 B cell epitopes, 9 SARS-CoV -2 epitopes, SARS-CoV -2 proteome, ORF 8 proteins

الوصف: Alignments were performed in Geneious Prime 2020.1.2 (Auckland, New Zealand). CoV, coronavirus; COVID-19, coronavirus disease 2019. (PDF)

العلاقة: https://figshare.com/articles/journal_contribution/Alignment_of_epitopes_in_human_and_animal_CoVs_for_which_antibodies_in_sera_from_40_COVID-19_convalescent_patients_showed_apparent_cross-reactive_binding_/14810135Test

الإتاحة: https://doi.org/10.1371/journal.pbio.3001265.s002Test

المؤلفون: Anna S. Heffron (6013853), Sean J. McIlwain (3221448), Maya F. Amjadi (10994525), David A. Baker (7494542), Saniya Khullar (10994528), Tammy Armbrust (7115156), Peter J. Halfmann (7115153), Yoshihiro Kawaoka (18302), Ajay K. Sethi (10994531), Ann C. Palmenberg (10994534), Miriam A. Shelef (5703491), David H. O’Connor (6639923), Irene M. Ong (8353449)

مصطلحات موضوعية: Biophysics, Biochemistry, Microbiology, Molecular Biology, Biotechnology, Evolutionary Biology, Immunology, Infectious Diseases, Virology, Computational Biology, Biological Sciences not elsewhere classified, Information Systems not elsewhere classified, peptide sequences, CoV proteins, syndrome coronavirus 2, SARS-CoV -2, SARS-CoV -2 infection bind, use ultradense peptide microarray m., SARS-CoV -2 infection, reactive B cell epitopes, Illness severity, enzyme-linked immunosorbent assay, Coronavirus membrane, humoral immunogens, ELISA, antibody responses, map 79 B cell epitopes, 9 SARS-CoV -2 epitopes, SARS-CoV -2 proteome, ORF 8 proteins

الوصف: Supporting information Table A contains the proteins represented on the array, including the GenBank accession numbers and the number of replicates of reach peptide in those proteins. Supporting information Table B contains the characteristics of the 40 COVID-19 convalescent patients and the 20 naïve controls whose sera were used in this study. Supporting information Table C contains the characteristics of the 40 COVID-19 convalescent patients according to hospitalization status. COVID-19, coronavirus disease 2019. (DOCX)

العلاقة: https://figshare.com/articles/journal_contribution/Supporting_information_tables_3_tables_show_data_relevant_to_the_Methods_for_this_study_/14810165Test

الإتاحة: https://doi.org/10.1371/journal.pbio.3001265.s012Test

المؤلفون: Anna S Heffron, Sean J McIlwain, Maya F Amjadi, David A Baker, Saniya Khullar, Tammy Armbrust, Peter J Halfmann, Yoshihiro Kawaoka, Ajay K Sethi, Ann C Palmenberg, Miriam A Shelef, David H O'Connor, Irene M Ong

المصدر: PLoS Biology, Vol 19, Iss 6, p e3001265 (2021)

مصطلحات موضوعية: Biology (General), QH301-705.5

الوصف: The search for potential antibody-based diagnostics, vaccines, and therapeutics for pandemic severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has focused almost exclusively on the spike (S) and nucleocapsid (N) proteins. Coronavirus membrane (M), ORF3a, and ORF8 proteins are humoral immunogens in other coronaviruses (CoVs) but remain largely uninvestigated for SARS-CoV-2. Here, we use ultradense peptide microarray mapping to show that SARS-CoV-2 infection induces robust antibody responses to epitopes throughout the SARS-CoV-2 proteome, particularly in M, in which 1 epitope achieved excellent diagnostic accuracy. We map 79 B cell epitopes throughout the SARS-CoV-2 proteome and demonstrate that antibodies that develop in response to SARS-CoV-2 infection bind homologous peptide sequences in the 6 other known human CoVs. We also confirm reactivity against 4 of our top-ranking epitopes by enzyme-linked immunosorbent assay (ELISA). Illness severity correlated with increased reactivity to 9 SARS-CoV-2 epitopes in S, M, N, and ORF3a in our population. Our results demonstrate previously unknown, highly reactive B cell epitopes throughout the full proteome of SARS-CoV-2 and other CoV proteins.

العلاقة: https://doi.org/10.1371/journal.pbio.3001265Test; https://doaj.org/toc/1544-9173Test; https://doaj.org/toc/1545-7885Test; https://doaj.org/article/b9d88ec1895f47f585722c14268539f4Test

الإتاحة: https://doi.org/10.1371/journal.pbio.3001265Test
https://doaj.org/article/b9d88ec1895f47f585722c14268539f4Test

المؤلفون: Kelly Watters, Ann C Palmenberg

المصدر: PLoS Pathogens, Vol 14, Iss 12, p e1007477 (2018)

مصطلحات موضوعية: Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5

الوصف: Viruses in the rhinovirus C species (RV-C) are more likely to cause severe wheezing illnesses and asthma exacerbations in children than related isolates of the RV-A or RV-B. The RV-C capsid is structurally distinct from other rhinoviruses and does not bind ICAM-1 or LDL receptors. The RV-C receptor is instead, human cadherin-related family member 3 (CDHR3), a protein unique to the airway epithelium. A single nucleotide polymorphism (rs6967330, encoding C529Y) in CDHR3 regulates the display density of CDHR3 on cell surfaces and is among the strongest known genetic correlates for childhood virus-induced asthma susceptibility. CDHR3 immunoprecipitations from transfected or transduced cell lysates were used to characterize the RV-C interaction requirements. The C529 and Y529 variations in extracellular repeat domain 5 (EC5), bound equivalently to virus. Glycosylase treatment followed by mass spectrometry mapped 3 extracellular N-linked modification sites, and further detected surface-dependent, α2-6 sialyation unique to the Y529 format. None of these modifications were required for RV-C recognition, but removal or even dilution of structurally stabilizing calcium ions from the EC junctions irreversibly abrogated virus binding. CDHR3 deletions expressed in HeLa cells or as bacterial recombinant proteins, mapped the amino-terminal EC1 unit as the required virus contact. Derivatives containing the EC1 domain, could not only recapitulate virus:receptor interactions in vitro, but also directly inhibit RV-C infection of susceptible cells for several virus genotypes (C02, C15, C41, and C45). We propose that all RV-C use the same EC1 landing pad, interacting with putative EC3-mediated multimerization formats of CDHR3.

العلاقة: https://doi.org/10.1371/journal.ppat.1007477Test; https://doaj.org/toc/1553-7366Test; https://doaj.org/toc/1553-7374Test; https://doaj.org/article/bfaf411ec2fc42f7bfc1fe92e96cdfceTest

الإتاحة: https://doi.org/10.1371/journal.ppat.1007477Test
https://doaj.org/article/bfaf411ec2fc42f7bfc1fe92e96cdfceTest

المؤلفون: Ann C. Palmenberg, Robert F. Kalejta

المصدر: J Virol

مصطلحات موضوعية: 0303 health sciences, Series (stratigraphy), 030306 microbiology, Immunology, Biology, Microbiology, Virology, Representation (politics), 03 medical and health sciences, Insect Science, Commentary, Parity (mathematics), Inclusion (education), 030304 developmental biology

الوصف: Historically, men rather than women have been selected for invited speaking positions at the four prominent virology conference series we have followed since the 1980s. However, the low ratio of female representation in most earlier years (20% in 1982 to 2010) has shown encouraging improvement (37% in 2011 to 2017), particularly over the last few years (48% in 2018 to 2020). Here, we describe this promising rise in inclusion and discuss factors that may help perpetuate and extend this overdue transformation toward gender parity.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a86ad27e58a1d7d80fbebaee16e8bf0Test
https://pubmed.ncbi.nlm.nih.gov/33762415Test

المؤلفون: Woonghee Lee, Kelly E Watters, Andrew T Troupis, Nichole M Reinen, Fabian P Suchy, Kylie L Moyer, Ronnie O Frederick, Marco Tonelli, David J Aceti, Ann C Palmenberg, John L Markley

المصدر: PLoS ONE, Vol 9, Iss 6, p e97198 (2014)

مصطلحات موضوعية: Medicine, Science

الوصف: Human rhinovirus strains differ greatly in their virulence, and this has been correlated with the differing substrate specificity of the respective 2A protease (2Apro). Rhinoviruses use their 2Apro to cleave a spectrum of cellular proteins important to virus replication and anti-host activities. These enzymes share a chymotrypsin-like fold stabilized by a tetra-coordinated zinc ion. The catalytic triad consists of conserved Cys (C105), His (H34), and Asp (D18) residues. We used a semi-automated NMR protocol developed at NMRFAM to determine the solution structure of 2Apro (C105A variant) from an isolate of the clinically important rhinovirus C species (RV-C). The backbone of C2 2Apro superimposed closely (1.41-1.81 Å rmsd) with those of orthologs from RV-A2, coxsackie B4 (CB4), and enterovirus 71 (EV71) having sequence identities between 40% and 60%. Comparison of the structures suggest that the differential functional properties of C2 2Apro stem from its unique surface charge, high proportion of surface aromatics, and sequence surrounding the di-tyrosine flap.

العلاقة: http://europepmc.org/articles/PMC4061012?pdf=renderTest; https://doaj.org/toc/1932-6203Test; https://doaj.org/article/943f24431a2749f3bb299b7fa9fca771Test

الإتاحة: https://doi.org/10.1371/journal.pone.0097198Test
https://doaj.org/article/943f24431a2749f3bb299b7fa9fca771Test