Hahn, Alexander S.

[["dc.bibliographiccitation.firstpage","2978"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","European Heart Journal"],["dc.bibliographiccitation.lastpage","2984"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Meyer, G. P."],["dc.contributor.author","Wollert, K. C."],["dc.contributor.author","Lotz, J."],["dc.contributor.author","Pirr, J."],["dc.contributor.author","Rager, U."],["dc.contributor.author","Lippolt, P."],["dc.contributor.author","Hahn, A."],["dc.contributor.author","Fichtner, S."],["dc.contributor.author","Schaefer, A."],["dc.contributor.author","Arseniev, L."],["dc.contributor.author","Drexler, H."],["dc.date.accessioned","2022-06-08T07:59:08Z"],["dc.date.available","2022-06-08T07:59:08Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1093/eurheartj/ehp374"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/110643"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.relation.eissn","1522-9645"],["dc.relation.issn","0195-668X"],["dc.title","Intracoronary bone marrow cell transfer after myocardial infarction: 5-year follow-up from the randomized-controlled BOOST trial"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Viruses"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Full, Florian"],["dc.contributor.author","Hahn, Alexander S."],["dc.contributor.author","Großkopf, Anna K."],["dc.contributor.author","Ensser, Armin"],["dc.date.accessioned","2019-07-09T11:44:45Z"],["dc.date.available","2019-07-09T11:44:45Z"],["dc.date.issued","2017-10-21"],["dc.description.abstract","Gammaherpesviruses like Epstein-Barr virus (EBV) and Kaposi's sarcoma-associated herpesvirus (KSHV) subvert the ubiquitin proteasome system for their own benefit in order to facilitate viral gene expression and replication. In particular, viral tegument proteins that share sequence homology to the formylglycineamide ribonucleotide amidotransferase (FGARAT, or PFAS), an enzyme in the cellular purine biosynthesis, are important for disrupting the intrinsic antiviral response associated with Promyelocytic Leukemia (PML) protein-associated nuclear bodies (PML-NBs) by proteasome-dependent and independent mechanisms. In addition, all herpesviruses encode for a potent ubiquitin protease that can efficiently remove ubiquitin chains from proteins and thereby interfere with several different cellular pathways. In this review, we discuss mechanisms and functional consequences of virus-induced ubiquitination and deubiquitination for early events in gammaherpesviral infection."],["dc.identifier.doi","10.3390/v9100308"],["dc.identifier.pmid","29065450"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14886"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59084"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1999-4915"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.subject.ddc","610"],["dc.title","Gammaherpesviral Tegument Proteins, PML-Nuclear Bodies and the Ubiquitin-Proteasome System."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1785"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Neurology"],["dc.bibliographiccitation.lastpage","1789"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Henneke, M."],["dc.contributor.author","Gegner, S."],["dc.contributor.author","Hahn, A."],["dc.contributor.author","Plecko-Startinig, B."],["dc.contributor.author","Weschke, B."],["dc.contributor.author","Gärtner, J."],["dc.contributor.author","Brockmann, K."],["dc.date.accessioned","2022-03-01T11:44:04Z"],["dc.date.available","2022-03-01T11:44:04Z"],["dc.date.issued","2010"],["dc.description.abstract","Background: Among the hypomyelinating leukoencephalopathies with onset in childhood, Pelizaeus-Merzbacher disease (PMD) and Pelizaeus-Merzbacher-like disease (PMLD) constitute a large subgroup with almost indistinguishable clinical and neuroradiologic features. Whereas PMD is due to X-linked PLP1 mutations, PMLD is genetically heterogeneous, with about 8% of patients carrying autosomal recessive GJA12/GJC2 mutations. The aim of this study was to evaluate whether neurophysiologic testing may separate PMD from GJA12/GJC2-associated PMLD. Methods: Retrospective data collection study with reevaluation of evoked potentials (EP) and nerve conduction studies (NCS) in 10 patients from 7 families with PMLD due to various GJA12/GJC2 mutations and 8 boys from 7 families with classic PMD caused by a PLP1 duplication or missense mutation. Results: In brainstem auditory EP, waves III-V were absent in all patients with PMD, but clearly recordable in 11 of 13 investigations in 8 patients with PMLD. Visual evoked potentials and somatosensory evoked potentials revealed conduction delay in both PMD and PMLD, without significant difference. NCS were normal in all patients with PMD and indicated mild peripheral neuropathy in only 2 of 10 patients with PMLD. Conclusion: In a patient with clinical and neuroradiologic features of Pelizaeus-Merzbacher disease/Pelizaeus-Merzbacher-like disease and a pedigree consistent with both conditions, brainstem auditory evoked potentials provide good selectivity between these disorders and point in the right direction for identifying the primary genetic defect. Neurology(R) 2010;74:1785-1789"],["dc.identifier.doi","10.1212/WNL.0b013e3181e0f820"],["dc.identifier.gro","3142917"],["dc.identifier.isi","000278154800007"],["dc.identifier.pmid","20513814"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102918"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.eissn","1526-632X"],["dc.relation.issn","0028-3878"],["dc.title","Clinical neurophysiology in GJA12-related hypomyelination vs Pelizaeus-Merzbacher disease"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2507"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Archives of Virology"],["dc.bibliographiccitation.lastpage","2512"],["dc.bibliographiccitation.volume","163"],["dc.contributor.author","Ensser, Armin"],["dc.contributor.author","Großkopf, Anna K."],["dc.contributor.author","Mätz-Rensing, Kerstin"],["dc.contributor.author","Roos, Christian"],["dc.contributor.author","Hahn, Alexander S."],["dc.date.accessioned","2018-11-28T13:57:57Z"],["dc.date.available","2018-11-28T13:57:57Z"],["dc.date.issued","2018"],["dc.description.abstract","SFVmmu-DPZ9524 represents the third completely sequenced rhesus macaque simian foamy virus (SFV) isolate, alongside SFVmmu_K3T with a similar SFV-1-type env, and R289HybAGM with a SFV-2-like env. Sequence analysis demonstrates that, in gag and pol, SFVmmu-DPZ9524 is more closely related to R289HybAGM than to SFVmmu_K3T, which, outside of env, is more similar to a Japanese macaque isolate than to the other two rhesus macaque isolates SFVmmu-DPZ9524 and R289HybAGM. Further, we identify bel as another recombinant locus in R289HybAGM, confirming that recombination contributes to sequence diversity in SFV."],["dc.identifier.doi","10.1007/s00705-018-3892-9"],["dc.identifier.pmid","29860676"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56996"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1432-8798"],["dc.title","Isolation and sequence analysis of a novel rhesus macaque foamy virus isolate with a serotype-1-like env"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8013"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.lastpage","8028"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Hahn, Alexander S."],["dc.contributor.author","Großkopf, Anna K."],["dc.contributor.author","Jungnickl, Doris"],["dc.contributor.author","Scholz, Brigitte"],["dc.contributor.author","Ensser, Armin"],["dc.contributor.editor","Jung, J. U."],["dc.date.accessioned","2022-10-06T13:25:34Z"],["dc.date.available","2022-10-06T13:25:34Z"],["dc.date.issued","2016"],["dc.description.abstract","ABSTRACT\n \n Nuclear domain 10 (ND10) components restrict herpesviral infection, and herpesviruses antagonize this restriction by a variety of strategies, including degradation or relocalization of ND10 proteins. The rhesus monkey rhadinovirus (RRV) shares many key biological features with the closely related Kaposi's sarcoma-associated herpesvirus (KSHV; human herpesvirus 8) and readily infects cells of both human and rhesus monkey origin. We used the clustered regularly interspaced short palindromic repeat-Cas9 (CRISPR-Cas9) technique to generate knockout (ko) cells for each of the four ND10 components, PML, SP100, DAXX, and ATRX. These ko cells were analyzed with regard to permissiveness for RRV infection. In addition, we analyzed the fate of the individual ND10 components in infected cells by immunofluorescence and Western blotting. Knockout of the ND10 component DAXX markedly increased RRV infection, while knockout of PML or SP100 had a less pronounced effect. In line with these observations, RRV infection resulted in rapid degradation of SP100, followed by degradation of PML and the loss of ND10 structures, whereas the protein levels of ATRX and DAXX remained constant. Notably, inhibition of the proteasome but not inhibition of\n de novo\n gene expression prevented the loss of SP100 and PML in cells that did not support lytic replication, compatible with proteasomal degradation of these ND10 components through the action of a viral tegument protein. Expression of the RRV FGARAT homolog ORF75 was sufficient to effect the loss of SP100 and PML in transfected or transduced cells, implicating ORF75 as the viral effector protein.\n \n \n IMPORTANCE\n Our findings highlight the antiviral role of ND10 and its individual components and further establish the viral FGARAT homologs of the gammaherpesviruses to be important viral effectors that counteract ND10-instituted intrinsic immunity. Surprisingly, even closely related viruses like KSHV and RRV evolved to use different strategies to evade ND10-mediated restriction. RRV first targets SP100 for degradation and then targets PML with a delayed kinetic, a strategy which clearly differs from that of other gammaherpesviruses. Despite efficient degradation of these two major ND10 components, RRV is still restricted by DAXX, another abundant ND10 component, as evidenced by a marked increase in RRV infection and replication upon knockout of DAXX. Taken together, our findings substantiate PML, SP100, and DAXX as key antiviral proteins, in that the first two are targeted for degradation by RRV and the last one still potently restricts replication of RRV."],["dc.identifier.doi","10.1128/JVI.01181-16"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114871"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","Viral FGARAT Homolog ORF75 of Rhesus Monkey Rhadinovirus Effects Proteasomal Degradation of the ND10 Components SP100 and PML"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e00002-21"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.volume","95"],["dc.contributor.author","Hörnich, Bojan F."],["dc.contributor.author","Großkopf, Anna K."],["dc.contributor.author","Schlagowski, Sarah"],["dc.contributor.author","Tenbusch, Matthias"],["dc.contributor.author","Kleine-Weber, Hannah"],["dc.contributor.author","Neipel, Frank"],["dc.contributor.author","Stahl-Hennig, Christiane"],["dc.contributor.author","Hahn, Alexander S."],["dc.contributor.editor","Gallagher, Tom"],["dc.date.accessioned","2022-10-06T13:25:30Z"],["dc.date.available","2022-10-06T13:25:30Z"],["dc.date.issued","2021"],["dc.description.abstract","Cell-cell fusion allows viruses to infect neighboring cells without the need to produce free virus and contributes to tissue damage by creating virus-infected syncytia. Our results demonstrate that the S2′ cleavage site is essential for activation by TMPRSS2 and unravel important differences between SARS-CoV and SARS-CoV-2, among those, greater dependence of SARS-CoV-2 on ACE2 expression and activation by metalloproteases for cell-cell fusion."],["dc.description.abstract","ABSTRACT\n Severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) infects cells through interaction of its spike protein (SARS2-S) with angiotensin-converting enzyme 2 (ACE2) and activation by proteases, in particular transmembrane protease serine 2 (TMPRSS2). Viruses can also spread through fusion of infected with uninfected cells. We compared the requirements of ACE2 expression, proteolytic activation, and sensitivity to inhibitors for SARS2-S-mediated and SARS-CoV-S (SARS1-S)-mediated cell-cell fusion. SARS2-S-driven fusion was moderately increased by TMPRSS2 and strongly by ACE2, while SARS1-S-driven fusion was strongly increased by TMPRSS2 and less so by ACE2 expression. In contrast to that of SARS1-S, SARS2-S-mediated cell-cell fusion was efficiently activated by batimastat-sensitive metalloproteases. Mutation of the S1/S2 proteolytic cleavage site reduced effector cell-target cell fusion when ACE2 or TMPRSS2 was limiting and rendered SARS2-S-driven cell-cell fusion more dependent on TMPRSS2. When both ACE2 and TMPRSS2 were abundant, initial target cell-effector cell fusion was unaltered compared to that of wild-type (wt) SARS2-S, but syncytia remained smaller. Mutation of the S2 cleavage (S2′) site specifically abrogated activation by TMPRSS2 for both cell-cell fusion and SARS2-S-driven pseudoparticle entry but still allowed for activation by metalloproteases for cell-cell fusion and by cathepsins for particle entry. Finally, we found that the TMPRSS2 inhibitor bromhexine, unlike the inhibitor camostat, was unable to reduce TMPRSS2-activated cell-cell fusion by SARS1-S and SARS2-S. Paradoxically, bromhexine enhanced cell-cell fusion in the presence of TMPRSS2, while its metabolite ambroxol exhibited inhibitory activity under some conditions. On Calu-3 lung cells, ambroxol weakly inhibited SARS2-S-driven lentiviral pseudoparticle entry, and both substances exhibited a dose-dependent trend toward weak inhibition of authentic SARS-CoV-2.\n \n IMPORTANCE\n Cell-cell fusion allows viruses to infect neighboring cells without the need to produce free virus and contributes to tissue damage by creating virus-infected syncytia. Our results demonstrate that the S2′ cleavage site is essential for activation by TMPRSS2 and unravel important differences between SARS-CoV and SARS-CoV-2, among those, greater dependence of SARS-CoV-2 on ACE2 expression and activation by metalloproteases for cell-cell fusion. Bromhexine, reportedly an inhibitor of TMPRSS2, is currently being tested in clinical trials against coronavirus disease 2019. Our results indicate that bromhexine enhances fusion under some conditions. We therefore caution against the use of bromhexine in high dosages until its effects on SARS-CoV-2 spike activation are better understood. The related compound ambroxol, which similarly to bromhexine is clinically used as an expectorant, did not exhibit activating effects on cell-cell fusion. Both compounds exhibited weak inhibitory activity against SARS-CoV-2 infection at high concentrations, which might be clinically attainable for ambroxol."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft https://doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Wilhelm Sander-Stiftung https://doi.org/10.13039/100008672"],["dc.identifier.doi","10.1128/JVI.00002-21"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114857"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://doi.org/10.1128/ASMCopyrightv2"],["dc.title","SARS-CoV-2 and SARS-CoV Spike-Mediated Cell-Cell Fusion Differ in Their Requirements for Receptor Expression and Proteolytic Activation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1552"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Emerging Infectious Diseases"],["dc.bibliographiccitation.lastpage","1555"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Grewer, Anna"],["dc.contributor.author","Bleyer, Martina"],["dc.contributor.author","Mätz-Rensing, Kerstin"],["dc.contributor.author","Hahn, Alexander S."],["dc.contributor.author","Rüggeberg, Tim"],["dc.contributor.author","Babaryka, Gregor"],["dc.contributor.author","Zimmermann, Andre"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Kaul, Artur"],["dc.date.accessioned","2020-12-10T18:44:08Z"],["dc.date.available","2020-12-10T18:44:08Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3201/eid2508.181804"],["dc.identifier.eissn","1080-6059"],["dc.identifier.issn","1080-6040"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78340"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Kaposi Sarcoma in Mantled Guereza"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0265453"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS One"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Arora, Prerna"],["dc.contributor.author","Sidarovich, Anzhalika"],["dc.contributor.author","Graichen, Luise"],["dc.contributor.author","Hörnich, Bojan"],["dc.contributor.author","Hahn, Alexander"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.editor","Bogyo, Matthew"],["dc.date.accessioned","2022-04-01T10:02:01Z"],["dc.date.available","2022-04-01T10:02:01Z"],["dc.date.issued","2022"],["dc.description.abstract","Several SARS-CoV-2 variants emerged that harbor mutations in the surface unit of the viral spike (S) protein that enhance infectivity and transmissibility. Here, we analyzed whether ten naturally-occurring mutations found within the extended loop harboring the S1/S2 cleavage site of the S protein, a determinant of SARS-CoV-2 cell tropism and pathogenicity, impact S protein processing and function. None of the mutations increased but several decreased S protein cleavage at the S1/S2 site, including S686G and P681H, the latter of which is found in variants of concern B.1.1.7 (Alpha variant) and B.1.1.529 (Omicron variant). None of the mutations reduced ACE2 binding and cell-cell fusion although several modulated the efficiency of host cell entry. The effects of mutation S686G on viral entry were cell-type dependent and could be linked to the availability of cathepsin L for S protein activation. These results show that polymorphisms at the S1/S2 site can modulate S protein processing and host cell entry."],["dc.identifier.doi","10.1371/journal.pone.0265453"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/105803"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1932-6203"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Functional analysis of polymorphisms at the S1/S2 site of SARS-CoV-2 spike protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e01093-19"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.volume","94"],["dc.contributor.author","Hahn, Alexander S."],["dc.contributor.author","Bischof, Georg F."],["dc.contributor.author","Großkopf, Anna K."],["dc.contributor.author","Shin, Young C."],["dc.contributor.author","Domingues, Aline"],["dc.contributor.author","Gonzalez-Nieto, Lucas"],["dc.contributor.author","Rakasz, Eva G."],["dc.contributor.author","Watkins, David I."],["dc.contributor.author","Ensser, Armin"],["dc.contributor.author","Martins, Mauricio A."],["dc.contributor.editor","Longnecker, Richard M."],["dc.date.accessioned","2022-10-06T13:25:34Z"],["dc.date.available","2022-10-06T13:25:34Z"],["dc.date.issued","2020"],["dc.description.abstract","Kaposi’s sarcoma-associated herpesvirus (KSHV) is associated with a substantial disease burden in sub-Saharan Africa, often in the context of human immunodeficiency virus (HIV) infection. The related rhesus monkey rhadinovirus (RRV) has shown potential as a vector to immunize monkeys with antigens from simian immunodeficiency virus (SIV), the macaque model for HIV. KSHV and RRV engage cellular receptors from the Eph family via the viral gH/gL glycoprotein complex. We have now generated a recombinant RRV that expresses the SIV Gag antigen and does not express gL. This recombinant RRV was infectious by the intravenous route, established persistent infection in the B cell compartment, and elicited strong immune responses to the SIV Gag antigen. These results argue against a role for gL and Eph family receptors in B cell infection by RRV\n in vivo\n and have implications for the development of a live-attenuated KSHV vaccine or vaccine vector."],["dc.description.abstract","ABSTRACT\n \n A replication-competent, recombinant strain of rhesus monkey rhadinovirus (RRV) expressing the Gag protein of SIVmac239 was constructed in the context of a glycoprotein L (gL) deletion mutation. Deletion of gL detargets the virus from Eph family receptors. The ability of this gL-minus Gag recombinant RRV to infect, persist, and elicit immune responses was evaluated after intravenous inoculation of two\n Mamu-A*01\n +\n RRV-naive rhesus monkeys. Both monkeys responded with an anti-RRV antibody response, and quantitation of RRV DNA in peripheral blood mononuclear cells (PBMC) by real-time PCR revealed levels similar to those in monkeys infected with recombinant gL\n +\n RRV. Comparison of RRV DNA levels in sorted CD3\n +\n versus CD20\n +\n versus CD14\n +\n PBMC subpopulations indicated infection of the CD20\n +\n subpopulation by the gL-minus RRV. This contrasts with results obtained with transformed B cell lines\n in vitro\n , in which deletion of gL resulted in markedly reduced infectivity. Over a period of 20 weeks, Gag-specific CD8\n +\n T cell responses were documented by major histocompatibility complex class I (MHC-I) tetramer staining. Vaccine-induced CD8\n +\n T cell responses, which were predominantly directed against the Mamu-A*01-restricted Gag\n 181-189\n CM9 epitope, could be inhibited by blockade of MHC-I presentation. Our results indicate that gL and the interaction with Eph family receptors are dispensable for the colonization of the B cell compartment following high-dose infection by the intravenous route, which suggests the existence of alternative receptors. Further, gL-minus RRV elicits cellular immune responses that are predominantly canonical in nature.\n \n \n IMPORTANCE\n Kaposi’s sarcoma-associated herpesvirus (KSHV) is associated with a substantial disease burden in sub-Saharan Africa, often in the context of human immunodeficiency virus (HIV) infection. The related rhesus monkey rhadinovirus (RRV) has shown potential as a vector to immunize monkeys with antigens from simian immunodeficiency virus (SIV), the macaque model for HIV. KSHV and RRV engage cellular receptors from the Eph family via the viral gH/gL glycoprotein complex. We have now generated a recombinant RRV that expresses the SIV Gag antigen and does not express gL. This recombinant RRV was infectious by the intravenous route, established persistent infection in the B cell compartment, and elicited strong immune responses to the SIV Gag antigen. These results argue against a role for gL and Eph family receptors in B cell infection by RRV\n in vivo\n and have implications for the development of a live-attenuated KSHV vaccine or vaccine vector."],["dc.description.sponsorship","IZKF Erlangen"],["dc.description.sponsorship"," HHS | National Institutes of Health https://doi.org/10.13039/100000002"],["dc.description.sponsorship"," HHS | National Institutes of Health https://doi.org/10.13039/100000002"],["dc.description.sponsorship"," HHS | National Institutes of Health https://doi.org/10.13039/100000002"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft https://doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft https://doi.org/10.13039/501100001659"],["dc.description.sponsorship"," HHS | U.S. Public Health Service https://doi.org/10.13039/100007197"],["dc.identifier.doi","10.1128/JVI.01093-19"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114870"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","A Recombinant Rhesus Monkey Rhadinovirus Deleted of Glycoprotein L Establishes Persistent Infection of Rhesus Macaques and Elicits Conventional T Cell Responses"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2384"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","2393.e12"],["dc.bibliographiccitation.volume","184"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Arora, Prerna"],["dc.contributor.author","Groß, Rüdiger"],["dc.contributor.author","Seidel, Alina"],["dc.contributor.author","Hörnich, Bojan F."],["dc.contributor.author","Hahn, Alexander S."],["dc.contributor.author","Krüger, Nadine"],["dc.contributor.author","Graichen, Luise"],["dc.contributor.author","Hofmann-Winkler, Heike"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2021-06-01T09:41:13Z"],["dc.date.available","2021-06-01T09:41:13Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.cell.2021.03.036"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84851"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.issn","0092-8674"],["dc.title","SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]