Biomolecular NMR Assignments最新文献

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1H, 15N, and 13C resonance assignments of the N-terminal domain and ser-arg-rich intrinsically disordered region of the nucleocapsid protein of the SARS-CoV-2 SARS-CoV-2 核苷酸蛋白 N 端结构域和富含 ser-arg 的内在无序区的 1H、15N 和 13C 共振赋值。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-08-22 DOI: 10.1007/s12104-024-10191-5
Peter R. Bezerra, Ariana A. Vasconcelos, Vitor S. Almeida, Thais C. Neves-Martins, Nathane C. Mebus-Antunes, Fabio C. L. Almeida
{"title":"1H, 15N, and 13C resonance assignments of the N-terminal domain and ser-arg-rich intrinsically disordered region of the nucleocapsid protein of the SARS-CoV-2","authors":"Peter R. Bezerra,&nbsp;Ariana A. Vasconcelos,&nbsp;Vitor S. Almeida,&nbsp;Thais C. Neves-Martins,&nbsp;Nathane C. Mebus-Antunes,&nbsp;Fabio C. L. Almeida","doi":"10.1007/s12104-024-10191-5","DOIUrl":"10.1007/s12104-024-10191-5","url":null,"abstract":"<div><p>The nucleocapsid (N) protein of SARS-CoV-2 is a multifunctional protein involved in nucleocapsid assembly and various regulatory functions. It is the most abundant protein during viral infection. Its functionality is closely related to its structure, which comprises two globular domains, the N-terminal domain (NTD) and the C-terminal domain (CTD), flanked by intrinsically disordered regions. The linker between the NTD and CTD includes a Serine-Arginine rich (SR) region, which is crucial for the regulation of the N protein’s function. Here, we report the near-complete assignment of the construct containing the NTD followed by the SR region (NTD-SR). Additionally, we describe the dynamic nature of the SR region and compare it with all other available chemical shift assignments reported for the SR region.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"219 - 225"},"PeriodicalIF":0.8,"publicationDate":"2024-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142034831","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
1H, 13C and 15N resonance assignments of a shark variable new antigen receptor against hyaluronan synthase 针对透明质酸合成酶的鲨鱼可变新抗原受体的 1H、13C 和 15N 共振分配。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-08-14 DOI: 10.1007/s12104-024-10190-6
Yuxin Liu, Hao Wang, Cookson K. C. Chiu, Yujie Wu, Yunchen Bi
{"title":"1H, 13C and 15N resonance assignments of a shark variable new antigen receptor against hyaluronan synthase","authors":"Yuxin Liu,&nbsp;Hao Wang,&nbsp;Cookson K. C. Chiu,&nbsp;Yujie Wu,&nbsp;Yunchen Bi","doi":"10.1007/s12104-024-10190-6","DOIUrl":"10.1007/s12104-024-10190-6","url":null,"abstract":"<div><p>Single domain antibody (sdAb) is only composed of a variable domain of the heavy-chain-only antibody, which is devoid of light chain and naturally occurring in camelids and cartilaginous fishes. Variable New Antigen Receptor (VNAR), a type of single domain antibody present in cartilaginous fishes such as sharks, is the smallest functional antigen-binding fragment found in nature. The unique features, including flexible paratope, high solubility and outstanding stability make VNAR a promising prospect in antibody drug development and structural biology research. However, VNAR’s research has lagged behind camelid-derived sdAb, especially in the field of structural research. Here we report the <sup>1</sup>H,<sup>15</sup>N,<sup>13</sup>C resonance assignments of a VNAR derived from the immune library of <i>Chiloscyllium plagiosum</i>, termed B2-3, which recognizes the hyaluronan synthase. Analysis of the backbone chemical shifts demonstrates that the secondary structure of VNAR is predominately composed of β-sheets corresponding to around 40% of the B2-3 backbone. The Cβ chemical shift values of cysteine residues, combined with mass spectrometry data, clearly shows that B2-3 contains two pairs of disulfide bonds, which is import for protein stability. The assignments will be essential for determining the high resolution solution structure of B2-3 by NMR spectroscopy.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"213 - 217"},"PeriodicalIF":0.8,"publicationDate":"2024-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141974792","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy 利用 MAS 固态 NMR 光谱手动和自动分配两种不同的 Aβ40 淀粉样蛋白纤维多态性。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-08-09 DOI: 10.1007/s12104-024-10189-z
Natalia Rodina, Riddhiman Sarkar, Dimitrios Tsakalos, Saba Suladze, Zheng Niu, Bernd Reif
{"title":"Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy","authors":"Natalia Rodina,&nbsp;Riddhiman Sarkar,&nbsp;Dimitrios Tsakalos,&nbsp;Saba Suladze,&nbsp;Zheng Niu,&nbsp;Bernd Reif","doi":"10.1007/s12104-024-10189-z","DOIUrl":"10.1007/s12104-024-10189-z","url":null,"abstract":"<div><p>Amyloid fibrils from Alzheimer’s amyloid-beta peptides (Aβ) are found to be polymorphic. So far, 14 Aβ40 fibril structures have been determined. The mechanism of why one particular protein sequence adopts so many different three-dimensional structures is yet not understood. In this work, we describe the assignment of the NMR chemical shifts of two Alzheimer’s disease fibril polymorphs, P1 and P2, which are formed by the amyloid-beta peptide Aβ40. The assignment is based on <sup>13</sup>C-detected 3D NCACX and NCOCX experiments MAS solid-state NMR experiments. The fibril samples are prepared using an extensive seeding protocol in the absence and presence of the small heat shock protein αB-crystallin. In addition to manual assignments, we obtain chemical shift assignments using the automation software ARTINA. We present an analysis of the secondary chemical shifts and a discussion on the differences between the manual and automated assignment strategies.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"201 - 212"},"PeriodicalIF":0.8,"publicationDate":"2024-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11511749/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141905490","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
1H, 13C and 15N assignment of self-complemented MrkA protein antigen from Klebsiella pneumoniae 肺炎克雷伯氏菌自补体 MrkA 蛋白抗原的 1H、13C 和 15N 赋值。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-07-17 DOI: 10.1007/s12104-024-10185-3
Valentina Monaci, Gianmarco Gasperini, Lucia Banci, Francesca Micoli, Francesca Cantini
{"title":"1H, 13C and 15N assignment of self-complemented MrkA protein antigen from Klebsiella pneumoniae","authors":"Valentina Monaci,&nbsp;Gianmarco Gasperini,&nbsp;Lucia Banci,&nbsp;Francesca Micoli,&nbsp;Francesca Cantini","doi":"10.1007/s12104-024-10185-3","DOIUrl":"10.1007/s12104-024-10185-3","url":null,"abstract":"<div><p>Klebsiella pneumoniae (Kp) poses an escalating threat to public health, particularly given its association with nosocomial infections and its emergence as a leading cause of neonatal sepsis, particularly in low- and middle-income countries (LMICs). Host cell adherence and biofilm formation of Kp is mediated by type 1 and type 3 fimbriae whose major fimbrial subunits are encoded by the <i>fimA</i> and <i>mrkA</i> genes, respectively. In this study, we focus on MrkA subunit, which is a 20 KDa protein whose 3D molecular structure remains elusive. We applied solution NMR to characterize a recombinant version of MrkA in which the donor strand segment situated at the protein’s N-terminus is relocated to the C-terminus, preceded by a hexaglycine linker. This construct yields a self-complemented variant of MrkA. Remarkably, the self-complemented MrkA monomer loses its capacity to interact with other monomers and to extend into fimbriae structures. Here, we report the nearly complete assignment of the <sup>13</sup>C,<sup>15</sup>N labelled self-complemented MrkA monomer. Furthermore, an examination of its internal mobility unveiled that relaxation parameters are predominantly uniform across the polypeptide sequence, except for the glycine-rich region within loop 176–181. These data pave the way to a comprehensive structural elucidation of the MrkA monomer and to structurally map the molecular interaction regions between MrkA and antigen-induced antibodies.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"171 - 179"},"PeriodicalIF":0.8,"publicationDate":"2024-07-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11511707/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141625602","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate 由螺旋中间体制备的α-突触核蛋白多晶体的固态核磁共振分配。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-07-04 DOI: 10.1007/s12104-024-10188-0
Sahil Ahlawat, Surabhi Mehra, Chandrakala M. Gowda, Samir K Maji, Vipin Agarwal
{"title":"Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate","authors":"Sahil Ahlawat,&nbsp;Surabhi Mehra,&nbsp;Chandrakala M. Gowda,&nbsp;Samir K Maji,&nbsp;Vipin Agarwal","doi":"10.1007/s12104-024-10188-0","DOIUrl":"10.1007/s12104-024-10188-0","url":null,"abstract":"<div><p>Synucleinopathies are neurodegenerative diseases characterized by the accumulation of α-synuclein protein aggregates in the neurons and glial cells. Both ex vivo and in vitro α-synuclein fibrils tend to show polymorphism. Polymorphism results in structure variations among fibrils originating from a single polypeptide/protein. The polymorphs usually have different biophysical, biochemical and pathogenic properties. The various pathologies of a single disease might be associated with distinct polymorphs. Similarly, in the case of different synucleinopathies, each condition might be associated with a different polymorph. Fibril formation is a nucleation-dependent process involving the formation of transient and heterogeneous intermediates from monomers. Polymorphs are believed to arise from heterogeneous oligomer populations because of distinct selection mechanisms in different conditions. To test this hypothesis, we isolated and incubated different intermediates during in vitro fibrillization of α-synuclein to form different polymorphs. Here, we report <sup>13</sup>C and <sup>15</sup>N chemical shifts and the secondary structure of fibrils prepared from the helical intermediate using solid-state nuclear magnetic spectroscopy.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"193 - 200"},"PeriodicalIF":0.8,"publicationDate":"2024-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11511750/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141496713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime 快速 MAS 机制下 α-突触核蛋白淀粉样纤维的固态 NMR 主干化学位移分配。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-06-29 DOI: 10.1007/s12104-024-10186-2
Zigmantas Toleikis, Piotr Paluch, Ewelina Kuc, Jana Petkus, Darius Sulskis, Mai-Liis Org-Tago, Ago Samoson, Vytautas Smirnovas, Jan Stanek, Alons Lends
{"title":"Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime","authors":"Zigmantas Toleikis,&nbsp;Piotr Paluch,&nbsp;Ewelina Kuc,&nbsp;Jana Petkus,&nbsp;Darius Sulskis,&nbsp;Mai-Liis Org-Tago,&nbsp;Ago Samoson,&nbsp;Vytautas Smirnovas,&nbsp;Jan Stanek,&nbsp;Alons Lends","doi":"10.1007/s12104-024-10186-2","DOIUrl":"10.1007/s12104-024-10186-2","url":null,"abstract":"<div><p>The α-synuclein (α-syn) amyloid fibrils are involved in various neurogenerative diseases. Solid-state NMR (ssNMR) has been showed as a powerful tool to study α-syn aggregates. Here, we report the <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N back-bone chemical shifts of a new α-syn polymorph obtained using proton-detected ssNMR spectroscopy under fast (95 kHz) magic-angle spinning conditions. The manual chemical shift assignments were cross-validated using FLYA algorithm. The secondary structural elements of α-syn fibrils were calculated using <sup>13</sup>C chemical shift differences and TALOS software.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"181 - 186"},"PeriodicalIF":0.8,"publicationDate":"2024-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141475633","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Backbone and methyl side-chain resonance assignments of the Fab fragment of adalimumab 阿达木单抗 Fab 片段的骨架和甲基侧链共振分配。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-06-26 DOI: 10.1007/s12104-024-10187-1
Muzaddid Sarker, Yves Aubin
{"title":"Backbone and methyl side-chain resonance assignments of the Fab fragment of adalimumab","authors":"Muzaddid Sarker,&nbsp;Yves Aubin","doi":"10.1007/s12104-024-10187-1","DOIUrl":"10.1007/s12104-024-10187-1","url":null,"abstract":"<div><p>Adalimumab is a therapeutic monoclonal antibody developed to target human TNF an important mediator of immune-mediated inflammatory diseases such as rheumatoid arthritis, amongst others. The 48 kDa Fab fragment of adalimumab was produced in <i>Escherichia coli</i> using a single chain approach to allow complete isotopic incorporation of deuterium, carbon-13 and nitrogen-15 along with the protonated isoleucine-d, valine and leucine methyl groups. Here we report the near complete resonance assignment of the polypeptide backbone and the methyl groups of isoleucine, leucine and valine residues.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"187 - 192"},"PeriodicalIF":0.8,"publicationDate":"2024-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11511761/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141454426","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Assignment of the Lassa virus transmembrane domain in the prefusion and postfusion states in detergent micelles 拉沙病毒跨膜结构域在洗涤剂胶束中的融合前和融合后状态的分配。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-06-25 DOI: 10.1007/s12104-024-10184-4
Patrick M. Keating, Jinwoo Lee
{"title":"Assignment of the Lassa virus transmembrane domain in the prefusion and postfusion states in detergent micelles","authors":"Patrick M. Keating,&nbsp;Jinwoo Lee","doi":"10.1007/s12104-024-10184-4","DOIUrl":"10.1007/s12104-024-10184-4","url":null,"abstract":"<div><p>Lassa virus (LASV) is the most prevalent member of the arenavirus family and the causative agent of Lassa fever, a viral hemorrhagic fever. Although there are annual outbreaks in West Africa, and recently isolated cases worldwide, there are no current therapeutics or vaccines. As such, LASV poses a significant global public health threat. One of the key steps in LASV infection is delivering its genetic material by fusing its viral membrane with the host cell membrane. This process is facilitated by significant conformational changes within glycoprotein 2 (GP2), yielding distinct prefusion and postfusion structural states. However, structural information is missing to understand the changes that occur in the transmembrane domain (TM) during the fusion process. Previously, we showed that the TM undergoes pH-dependent structural changes that result in a helical extension. Here, we provide the <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C assignment of the LASV TM backbone in the prefusion and postfusion states. We also provide the <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C assignment of two mutants, G429P and D432P, which prevent this helical extension. These results will help understand the role the TM plays in membrane fusion and can lead to the design of therapeutics against LASV infection.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"165 - 169"},"PeriodicalIF":0.8,"publicationDate":"2024-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141445096","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
NMR resonance assignment of the cell death execution domain BELL2 from multicellular bacterial signalosomes 多细胞细菌信号体中细胞死亡执行结构域 BELL2 的核磁共振分配。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-06-22 DOI: 10.1007/s12104-024-10183-5
Loic Delcourte, Corinne Sanchez, Estelle Morvan, Mélanie Berbon, Axelle Grélard, Claire Saragaglia, Thierry Dakhli, Stéphane Thore, Benjamin Bardiaux, Birgit Habenstein, Brice Kauffmann, Sven J. Saupe, Antoine Loquet
{"title":"NMR resonance assignment of the cell death execution domain BELL2 from multicellular bacterial signalosomes","authors":"Loic Delcourte,&nbsp;Corinne Sanchez,&nbsp;Estelle Morvan,&nbsp;Mélanie Berbon,&nbsp;Axelle Grélard,&nbsp;Claire Saragaglia,&nbsp;Thierry Dakhli,&nbsp;Stéphane Thore,&nbsp;Benjamin Bardiaux,&nbsp;Birgit Habenstein,&nbsp;Brice Kauffmann,&nbsp;Sven J. Saupe,&nbsp;Antoine Loquet","doi":"10.1007/s12104-024-10183-5","DOIUrl":"10.1007/s12104-024-10183-5","url":null,"abstract":"<div><p>Signalosomes are high-order protein machineries involved in complex mechanisms controlling regulated immune defense and cell death execution. The immune response is initiated by the recognition of exogeneous or endogenous signals, triggering the signalosome assembly process. The final step of signalosome fate often involves membrane-targeting and activation of pore-forming execution domains, leading to membrane disruption and ultimately cell death. Such cell death-inducing domains have been thoroughly characterized in plants, mammals and fungi, notably for the fungal cell death execution protein domain HeLo. However, little is known on the mechanisms of signalosome-based immune response in bacteria, and the conformation of cell death executors in bacterial signalosomes is still poorly characterized. We recently uncovered the existence of NLR signalosomes in various multicellular bacteria and used genome mining approaches to identify putative cell death executors in <i>Streptomyces olivochromogenes</i>. These proteins contain a C-terminal amyloid domain involved in signal transmission and a N-terminal domain, termed BELL for Bacteria analogous to fungal HeLL (HeLo-like), presumably responsible for membrane-targeting, pore-forming and cell death execution. In the present study, we report the high yield expression of <i>S. olivochromogenes</i> BELL2 and its characterization by solution NMR spectroscopy. BELL is folded in solution and we report backbone and sidechain assignments. We identified five α-helical secondary structure elements and a folded core much smaller than its fungal homolog HeLo. This study constitutes the first step toward the NMR investigation of the full-length protein assembly and its membrane targeting.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"159 - 164"},"PeriodicalIF":0.8,"publicationDate":"2024-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141439906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19 人类副病毒病原体 B19 的 VP1u N 端受体结合域的骨架核磁共振共振分配。
IF 0.8 4区 生物学
Biomolecular NMR Assignments Pub Date : 2024-06-21 DOI: 10.1007/s12104-024-10181-7
Maria Luiza Caldas Nogueira, Renuk Lakshmanan, Gwladys Rivière, Mario Mietzsch, Antonette Bennett, Robert McKenna, Joanna R. Long
{"title":"Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19","authors":"Maria Luiza Caldas Nogueira,&nbsp;Renuk Lakshmanan,&nbsp;Gwladys Rivière,&nbsp;Mario Mietzsch,&nbsp;Antonette Bennett,&nbsp;Robert McKenna,&nbsp;Joanna R. Long","doi":"10.1007/s12104-024-10181-7","DOIUrl":"10.1007/s12104-024-10181-7","url":null,"abstract":"<div><p>Parvovirus B19 (B19V) is a human pathogen that is the causative agent of several diseases in infants and adults. Due to a lack of antivirals against this virus, treatment options are limited. The minor capsid protein of B19V has a unique N terminus, named VP1u, which is essential for infection. The VP1u encodes a receptor binding domain (RBD), necessary for host cell entry, and a phospholipase A2 (PLA<sub>2</sub>) domain, crucial for endosomal escape during cellular trafficking. Both domains are indispensable for infection, making the RBD a plausible drug target for inhibitors against B19V, as it is located on the exterior surface of the virus. To date, no experimental structural information has been available for the VP1u component for any Parvovirus. Here we report the backbone NMR resonance assignments for the RBD of B19V and demonstrate it forms a stable structure. The backbone chemical shifts are in good agreement with a structure predicted by AlphaFold, validating that the RBD contains three helices connected by tight turns. This RBD construct can now be used for further NMR studies, including assignment of full-length VP1u, determination of protein-protein interaction interfaces, and development of B19 antivirals specific to the RBD domain.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"147 - 152"},"PeriodicalIF":0.8,"publicationDate":"2024-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141431063","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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