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Article ; Online: Author Correction: Protein-based profiling of the human IgA1 clonal repertoire revealed shared clones of serum polymeric IgA1 and milk secretory IgA1.

Novak, Jan / Renfrow, Matthew B / King, R Glenn / Reily, Colin / Green, Todd J

2024 Volume 20, Issue 3, Page(s) 310

Language	English
Publishing date	2024-02-21
Publishing country	China
Document type	Published Erratum
ZDB-ID	2435097-7
ISSN	2042-0226 ; 1672-7681
ISSN (online)	2042-0226
ISSN	1672-7681
DOI	10.1038/s41423-023-00977-3
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Article ; Online: GDP polyribonucleotidyltransferase domain of vesicular stomatitis virus polymerase regulates leader-promoter escape and polyadenylation-coupled termination during stop-start transcription.

Ogino, Minako / Green, Todd J / Ogino, Tomoaki

PLoS pathogens

2022 Volume 18, Issue 2, Page(s) e1010287

Abstract: The unconventional mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase) domain of the vesicular stomatitis virus (VSV) L protein possesses a dual-functional "priming-capping loop" that governs terminal de novo initiation for leader RNA ... ...

Abstract	The unconventional mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase) domain of the vesicular stomatitis virus (VSV) L protein possesses a dual-functional "priming-capping loop" that governs terminal de novo initiation for leader RNA synthesis and capping of monocistronic mRNAs during the unique stop-start transcription cycle. Here, we investigated the roles of basic amino acid residues on a helix structure directly connected to the priming-capping loop in viral RNA synthesis and identified single point mutations that cause previously unreported defective phenotypes at different steps of stop-start transcription. Mutations of residue R1183 (R1183A and R1183K) dramatically reduced the leader RNA synthesis activity by hampering early elongation, but not terminal de novo initiation or productive elongation, suggesting that the mutations negatively affect escape from the leader promoter. On the other hand, mutations of residue R1178 (R1178A and R1178K) decreased the efficiency of polyadenylation-coupled termination of mRNA synthesis at the gene junctions, but not termination of leader RNA synthesis at the leader-to-N-gene junction, resulting in the generation of larger amounts of aberrant polycistronic mRNAs. In contrast, both the R1183 and R1178 residues are not essential for cap-forming activities. The R1183K mutation was lethal to VSV, whereas the R1178K mutation attenuated VSV and triggered the production of the polycistronic mRNAs in infected cells. These observations suggest that the PRNTase domain plays multiple roles in conducting accurate stop-start transcription beyond its known role in pre-mRNA capping.
MeSH term(s)	Amino Acid Substitution ; Animals ; Cell Line ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Mutation ; Nucleotidyltransferases/metabolism ; Polyribonucleotide Nucleotidyltransferase/genetics ; Polyribonucleotide Nucleotidyltransferase/metabolism ; Protein Conformation ; Protein Domains ; RNA Precursors/metabolism ; RNA, Viral/metabolism ; RNA-Dependent RNA Polymerase/genetics ; RNA-Dependent RNA Polymerase/metabolism ; Transcription, Genetic ; Vesicular Stomatitis/virology ; Vesicular stomatitis Indiana virus/genetics ; Vesicular stomatitis Indiana virus/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication
Chemical Substances	RNA Precursors ; RNA, Viral ; Viral Proteins ; Nucleotidyltransferases (EC 2.7.7.-) ; L protein, vesicular stomatitis virus (EC 2.7.7.48) ; RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; mRNA guanylyltransferase (EC 2.7.7.50) ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Polyribonucleotide Nucleotidyltransferase (EC 2.7.7.8)
Language	English
Publishing date	2022-02-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010287
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Article ; Online: Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation.

Samal, Alexandra B / Green, Todd J / Saad, Jamil S

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 23, Page(s) e2200794119

Abstract: During the late phase of HIV type 1 (HIV-1) infection cycle, the virally encoded Gag polyproteins are targeted to the inner leaflet of the plasma membrane (PM) for assembly, formation of immature particles, and virus release. Gag binding to the PM is ... ...

Abstract	During the late phase of HIV type 1 (HIV-1) infection cycle, the virally encoded Gag polyproteins are targeted to the inner leaflet of the plasma membrane (PM) for assembly, formation of immature particles, and virus release. Gag binding to the PM is mediated by interactions of the N-terminally myristoylated matrix (myrMA) domain with phosphatidylinositol 4,5-bisphosphate. Formation of a myrMA lattice on the PM is an obligatory step for the assembly of immature HIV-1 particles and envelope (Env) incorporation. Atomic details of the myrMA lattice and how it mediates Env incorporation are lacking. Herein, we present the X-ray structure of myrMA at 2.15 Å. The myrMA lattice is arranged as a hexamer of trimers with a central hole, thought to accommodate the C-terminal tail of Env to promote incorporation into virions. The trimer–trimer interactions in the lattice are mediated by the N-terminal loop of one myrMA molecule and α-helices I–II, as well as the 310 helix of a myrMA molecule from an adjacent trimer. We provide evidence that substitution of MA residues Leu13 and Leu31, previously shown to have adverse effects on Env incorporation, induced a conformational change in myrMA, which may destabilize the trimer–trimer interactions within the lattice. We also show that PI(4,5)P2 is capable of binding to alternating sites on MA, consistent with an MA–membrane binding mechanism during assembly of the immature particle and upon maturation. Altogether, these findings advance our understanding of a key mechanism in HIV-1 particle assembly.
MeSH term(s)	Cell Membrane/metabolism ; HIV-1/metabolism ; Protein Domains ; Virion/metabolism ; Virus Assembly ; gag Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	gag Gene Products, Human Immunodeficiency Virus
Language	English
Publishing date	2022-06-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2200794119
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Article: RNA Synthesis and Capping by Non-segmented Negative Strand RNA Viral Polymerases: Lessons From a Prototypic Virus.

Ogino, Tomoaki / Green, Todd J

Frontiers in microbiology

2019 Volume 10, Page(s) 1490

Abstract: Non-segmented negative strand (NNS) RNA viruses belonging to the ... ...

Abstract	Non-segmented negative strand (NNS) RNA viruses belonging to the order
Language	English
Publishing date	2019-07-10
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2019.01490
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Article ; Online: Transcriptional Control and mRNA Capping by the GDP Polyribonucleotidyltransferase Domain of the Rabies Virus Large Protein.

Ogino, Tomoaki / Green, Todd J

Viruses

2019 Volume 11, Issue 6

Abstract: Rabies virus (RABV) is a causative agent of a fatal neurological disease in humans and animals. The large (L) protein of RABV is a multifunctional RNA-dependent RNA polymerase, which is one of the most attractive targets for developing antiviral agents. ... ...

Abstract	Rabies virus (RABV) is a causative agent of a fatal neurological disease in humans and animals. The large (L) protein of RABV is a multifunctional RNA-dependent RNA polymerase, which is one of the most attractive targets for developing antiviral agents. A remarkable homology of the RABV L protein to a counterpart in vesicular stomatitis virus, a well-characterized rhabdovirus, suggests that it catalyzes mRNA processing reactions, such as 5'-capping, cap methylation, and 3'-polyadenylation, in addition to RNA synthesis. Recent breakthroughs in developing in vitro RNA synthesis and capping systems with a recombinant form of the RABV L protein have led to significant progress in our understanding of the molecular mechanisms of RABV RNA biogenesis. This review summarizes functions of RABV replication proteins in transcription and replication, and highlights new insights into roles of an unconventional mRNA capping enzyme, namely GDP polyribonucleotidyltransferase, domain of the RABV L protein in mRNA capping and transcription initiation.
MeSH term(s)	Animals ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Gene Expression Regulation ; Genome, Viral ; Humans ; Polyribonucleotide Nucleotidyltransferase/genetics ; Polyribonucleotide Nucleotidyltransferase/metabolism ; RNA Caps/metabolism ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Rabies virus/chemistry ; Rabies virus/genetics ; Rabies virus/metabolism ; Rhabdoviridae/genetics ; Rhabdoviridae/metabolism ; Transcription, Genetic ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication
Chemical Substances	RNA Caps ; RNA, Viral ; Viral Proteins ; L protein, Rabies virus (EC 2.7.7.48) ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Polyribonucleotide Nucleotidyltransferase (EC 2.7.7.8)
Language	English
Publishing date	2019-06-01
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v11060504
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Article ; Online: Discontinuous L-binding motifs in the transactivation domain of the vesicular stomatitis virus P protein are required for terminal

Gupta, Nirmala / Ogino, Minako / Watkins, Dean E / Yu, Tiffany / Green, Todd J / Ogino, Tomoaki

Journal of virology

2023 Volume 97, Issue 8, Page(s) e0024623

Abstract: The phospho- (P) protein, the co-factor of the RNA polymerase large (L) protein, of vesicular stomatitis virus (VSV, a prototype of nonsegmented negative-strand RNA viruses) plays pivotal roles in transcription and replication. However, the precise ... ...

Abstract	The phospho- (P) protein, the co-factor of the RNA polymerase large (L) protein, of vesicular stomatitis virus (VSV, a prototype of nonsegmented negative-strand RNA viruses) plays pivotal roles in transcription and replication. However, the precise mechanism underlying the transcriptional transactivation by the P protein has remained elusive. Here, using an
MeSH term(s)	Animals ; Vesicular Stomatitis/genetics ; Transcriptional Activation ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Vesiculovirus/metabolism ; Vesicular stomatitis Indiana virus/genetics ; Vesicular stomatitis Indiana virus/metabolism ; RNA, Messenger/genetics ; Amino Acids/genetics ; Transcription, Genetic ; Virus Replication/genetics
Chemical Substances	RNA, Viral ; RNA, Messenger ; Amino Acids
Language	English
Publishing date	2023-08-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00246-23
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Zs.A 609: Show issues

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Article ; Online: Structure of Nonstructural Protein 1 from SARS-CoV-2.

Clark, Lauren K / Green, Todd J / Petit, Chad M

Journal of virology

2021 Volume 95, Issue 4

Abstract: The periodic emergence of novel coronaviruses (CoVs) represents an ongoing public health concern with significant health and financial burdens worldwide. The most recent occurrence originated in the city of Wuhan, China, where a novel coronavirus (severe ...

Abstract	The periodic emergence of novel coronaviruses (CoVs) represents an ongoing public health concern with significant health and financial burdens worldwide. The most recent occurrence originated in the city of Wuhan, China, where a novel coronavirus (severe acute respiratory syndrome coronavirus 2 [SARS-CoV-2]) emerged causing severe respiratory illness and pneumonia. The continual emergence of novel coronaviruses underscores the importance of developing effective vaccines as well as novel therapeutic options that target either viral functions or host factors recruited to support coronavirus replication. The CoV nonstructural protein 1 (nsp1) has been shown to promote cellular mRNA degradation, block host cell translation, and inhibit the innate immune response to virus infection. Interestingly, deletion of the nsp1-coding region in infectious clones prevented the virus from productively infecting cultured cells. Because of nsp1's importance in the CoV life cycle, it has been highlighted as a viable target for both antiviral therapy and vaccine development. However, the fundamental molecular and structural mechanisms that underlie nsp1 function remain poorly understood, despite its critical role in the viral life cycle. Here, we report the high-resolution crystal structure of the amino globular portion of SARS-CoV-2 nsp1 (residues 10 to 127) at 1.77-Å resolution. A comparison of our structure with the SARS-CoV-1 nsp1 structure reveals how mutations alter the conformation of flexible loops, inducing the formation of novel secondary structural elements and new surface features. Paired with the recently published structure of the carboxyl end of nsp1 (residues 148 to 180), our results provide the groundwork for future studies focusing on SARS-CoV-2 nsp1 structure and function during the viral life cycle.
MeSH term(s)	Amino Acid Sequence ; COVID-19/virology ; Cell Line ; Crystallography, X-Ray ; Humans ; Protein Conformation ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; Sequence Alignment ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/metabolism
Chemical Substances	NSP1 protein, SARS-CoV-2 ; Viral Nonstructural Proteins
Language	English
Publishing date	2021-01-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.02019-20
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Article ; Online: Neutrophil elastase-dependent cleavage of LTA4H alters its aminopeptidase activity in cystic fibrosis.

Xu, Xin / Li, Jin-Dong / Green, Todd J / Wilson, Landon / Genschmer, Kristopher / Russell, Derek / Blalock, J Edwin / Gaggar, Amit

The European respiratory journal

2024 Volume 63, Issue 3

MeSH term(s)	Humans ; Leukocyte Elastase ; Cystic Fibrosis ; Proteolysis ; Aminopeptidases/genetics ; Neutrophils
Chemical Substances	Leukocyte Elastase (EC 3.4.21.37) ; Aminopeptidases (EC 3.4.11.-)
Language	English
Publishing date	2024-03-07
Publishing country	England
Document type	Letter
ZDB-ID	639359-7
ISSN	1399-3003 ; 0903-1936
ISSN (online)	1399-3003
ISSN	0903-1936
DOI	10.1183/13993003.01512-2023
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Zs.A 2322: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Current Understanding of Complement Proteins as Therapeutic Targets for the Treatment of Immunoglobulin A Nephropathy.

Rajasekaran, Arun / Green, Todd J / Renfrow, Matthew B / Julian, Bruce A / Novak, Jan / Rizk, Dana V

Drugs

2023 Volume 83, Issue 16, Page(s) 1475–1499

Abstract: Immunoglobulin A nephropathy (IgAN) is the most common primary glomerulonephritis worldwide and a frequent cause of kidney failure. Currently, the diagnosis necessitates a kidney biopsy, with routine immunofluorescence microscopy revealing IgA as the ... ...

Abstract	Immunoglobulin A nephropathy (IgAN) is the most common primary glomerulonephritis worldwide and a frequent cause of kidney failure. Currently, the diagnosis necessitates a kidney biopsy, with routine immunofluorescence microscopy revealing IgA as the dominant or co-dominant immunoglobulin in the glomerular immuno-deposits, often with IgG and sometimes IgM or both. Complement protein C3 is observed in most cases. IgAN leads to kidney failure in 20-40% of patients within 20 years of diagnosis and reduces average life expectancy by about 10 years. There is increasing clinical, biochemical, and genetic evidence that the complement system plays a paramount role in the pathogenesis of IgAN. The presence of C3 in the kidney immuno-deposits differentiates the diagnosis of IgAN from subclinical glomerular mesangial IgA deposition. Markers of complement activation via the lectin and alternative pathways in kidney-biopsy specimens are associated with disease activity and are predictive of poor outcome. Levels of select complement proteins in the circulation have also been assessed in patients with IgAN and found to be of prognostic value. Ongoing genetic studies have identified at least 30 loci associated with IgAN. Genes within some of these loci encode complement-system regulating proteins that can interact with immune complexes. The growing appreciation for the central role of complement components in IgAN pathogenesis highlighted these pathways as potential treatment targets and sparked great interest in pharmacological agents targeting the complement cascade for the treatment of IgAN, as evidenced by the plethora of ongoing clinical trials.
MeSH term(s)	Humans ; Glomerulonephritis, IGA/drug therapy ; Kidney ; Complement C3 ; Immunoglobulin A ; Renal Insufficiency
Chemical Substances	Complement C3 ; Immunoglobulin A
Language	English
Publishing date	2023-09-25
Publishing country	New Zealand
Document type	Journal Article ; Review
ZDB-ID	120316-2
ISSN	1179-1950 ; 0012-6667
ISSN (online)	1179-1950
ISSN	0012-6667
DOI	10.1007/s40265-023-01940-2
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Article ; Online: Protein-based profiling of the human IgA1 clonal repertoire revealed shared clones of serum polymeric IgA1 and milk secretory IgA1.

Novak, Jan / Renfrow, Matthew B / King, R Glenn / Reily, Colin / Green, Todd J

Cellular & molecular immunology

2023 Volume 20, Issue 3, Page(s) 305–307

MeSH term(s)	Animals ; Humans ; Clone Cells ; Immunoglobulin A ; Immunoglobulin A, Secretory ; Milk
Chemical Substances	Immunoglobulin A ; Immunoglobulin A, Secretory
Language	English
Publishing date	2023-01-04
Publishing country	China
Document type	Research Support, N.I.H., Extramural ; Journal Article ; Comment
ZDB-ID	2435097-7
ISSN	2042-0226 ; 1672-7681
ISSN (online)	2042-0226
ISSN	1672-7681
DOI	10.1038/s41423-022-00965-z
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