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Robb, N. C.

Publications and source records attributed to Robb, N. C..

7 recordsLinked to original sources

Molecular and Structural Characterisation of the MERS-Coronavirus Polymerase

MERS-CoV (Middle East respiratory syndrome coronavirus) belongs to the Betacoronavirus genus, which also includes SARS-CoV-2, the causative agent of the COVID-19 pandemic. MERS-CoV is the pathogen responsible for Middle East Respiratory Syndrome (MERS), a respiratory disease with a 36.5% case fatality rate. Given the capacity of coronaviruses for genetic recombination and mutation, MERS-CoV remains a pathogen of significant pandemic potential, with viral evolution potentially facilitating enhanced adaptation and transmission in humans. There are no approved treatments for MERS-CoV infection. The MERS-CoV replication-transcription complex (RTC), a multimeric protein complex key to genome amplification, has no cellular analogues and a highly conserved sequence, making it a useful target for antiviral compounds; however, structural and biochemical characterisation of the MERS-CoV RTC is limited. Here, we characterise the minimal MERS-CoV RTC using in vitro and single-molecule assays and show that it is susceptible to the RNA-dependent-RNA-polymerase inhibitor suramin. We present a structure of the minimal MERS-CoV RTC in complex with an RNA duplex, which shows strong structural similarity to the SARS-CoV-2 RTC. We use cross-subunit swapping experiments to show that the MERS-CoV NSP12 core can efficiently utilise SARS-CoV-2 cofactors NSP7 and NSP8, whereas SARS-CoV-2 NSP12 exhibits reduced in vitro activity with the MERS-CoV NSP8. This asymmetric cross-species compatibility highlights both the evolutionary conservation and virus-specific adaptation of coronavirus polymerase-cofactor interactions. Together, these findings provide a structural and mechanistic framework for understanding MERS-CoV RNA synthesis and establish its conserved RTC as a potential target for the development of broadly acting coronavirus antivirals.

microbiology↗

Isothermal Detection of Influenza D using RT-LAMP

The Orthomyxoviridae family includes influenza D virus (IDV), an emerging pathogen primarily affecting cattle and swine, with evidence of cross-species transmission and potential zoonotic risk. Although active human infections have yet to been confirmed, high seroprevalence in cattle-exposed populations highlights the need for continued surveillance. Here, a rapid, field-deployable RT-LAMP assay for IDV detection was developed and validated, with 99.2% specificity and sensitivity ranging from 95.6% (Cq < 30) to 81.8% (Cq < 40). This method offers a cost-effective, accessible alternative to RT-qPCR, enabling improved monitoring of IDV, and reinforcing preparedness for emerging influenza threats.

microbiology↗

Bioinformatics-based stereochemical elucidation of MM 46115: an unusual antiviral spirotetronate that inhibits clathrin-mediated endocytosis

The influenza virus is a leading cause of respiratory tract infection in humans, with the emergence of antiviral drug resistance posing an ongoing challenge to the treatment of influenza. This underscores the urgent need for effective new antiviral treatments. Spirotetronates are a family of bacterial natural products with a range of potent bioactivities. Some members of this family have antiviral activity. Here, we report the bioinformatics-based stereochemical assignment, antiviral properties, and mechanism of action of the unusual type II spirotetronate MM 46115 (renamed pellemicin). We show that pellemicin is active against both influenza A and B viruses at non-toxic concentrations, and inhibits clathrin-mediated endocytosis, which is required for virus internalisation. Given the need for new treatments for viral infections, the results of our work suggest that pellemicin and related spirotetronates could provide a basis for developing promising alternatives to existing antivirals to combat drug-resistant influenza. Graphical abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=199 SRC="FIGDIR/small/677008v1_ufig1.gif" ALT="Figure 1"> View larger version (42K): org.highwire.dtl.DTLVardef@177aacforg.highwire.dtl.DTLVardef@16f0b26org.highwire.dtl.DTLVardef@144f9dcorg.highwire.dtl.DTLVardef@16fe673_HPS_FORMAT_FIGEXP M_FIG C_FIG HighlightsO_LIMM 46115 (here renamed pellemicin) produced by a mycetoma pathogen is a promising antiviral C_LIO_LIThe pellemicin biosynthetic gene cluster was identified in Actinomadura pelletieri DSM 43383 C_LIO_LISequence analysis of biosynthetic enzymes enabled full stereochemical assignment C_LIO_LIPellemicin inhibits clathrin-mediated endocytosis, an early stage of the viral life cycle C_LI SignificanceThe influenza virus is a respiratory pathogen with epidemic and pandemic potential, resulting in tens of thousands of deaths each year and causing significant health, social and economic impact. The rise of resistant influenza strains against existing antiviral drugs creates a pressing need for alternative treatments. Natural products - specialised metabolites of bacteria, fungi, and plants that often have antimicrobial activity - are a promising source of therapeutics to treat human disease. Here, we identify a cryptic polyketide biosynthetic gene cluster in the genome sequence of Actinomadura pelletieri DSM 43383, an Actinomycete that causes mycetoma in humans. This is proposed to direct production of the previously reported spirotetronate MM 46115 (here renamed pellemicin), which has activity against the influenza virus. Sequence analyses of a polyketide synthase and Diels-Alderase involved in pellemicin biosynthesis, combined with comparative analysis of NMR data for other spirotetronates, enabled us to fully resolve longstanding stereochemical ambiguities in the structure of pellemicin. This underscores the emerging power of bioinformatics-based approaches, and their complementarity to traditional spectroscopic methods, for natural product structure elucidation. We also report extensive insights into the antiviral properties and mechanism of pellemicin, demonstrating that it exhibits antiviral activity at non-toxic doses for up to eight hours after administration and inhibits clathrin-mediated endocytosis, a process that many viruses exploit to enter cells. Only one other bacterial natural product, ikarugamycin, is known to inhibit clathrin-mediated endocytosis. Ikarugamycin contains a tetramate group, which bears a close structural relationship to the tetronate moiety of pellemicin, suggesting that inhibition of clathrin-mediated endocytosis may be a general mechanism of action for antiviral spirotetronates. Our findings therefore indicate that pellemicin, and related spirotetronate natural products, could form a basis for development of new drugs to combat antiviral resistance, and serve as useful tools to study the process of endocytosis.

microbiology↗

Mechanistic insights into the activity of SARS-CoV-2 RNA polymerase inhibitors using single-molecule FRET

The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has resulted in significant global mortality and disruption. Despite extensive research, the precise molecular mechanisms underlying SARS-CoV-2 replication remain unclear. To address this, we developed a single-molecule Forster resonance energy transfer (smFRET) assay to directly visualize and analyse in vitro RNA synthesis by the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp). We purified the minimal replication complex, comprising nsp12, nsp7, and nsp8, and combined it with fluorescently labelled RNA substrates, enabling real-time monitoring of RNA primer elongation at the single-molecule level. This platform allowed us to investigate the mechanisms of action of key inhibitors of SARS-CoV-2 replication. In particular, our data provides evidence for remdesivirs mechanism of action, which involves polymerase stalling and subsequent chain termination dependent on the concentration of competing nucleotide triphosphates. Our study demonstrates the power of smFRET to provide dynamic insights into SARS-CoV-2 replication, offering a valuable tool for antiviral screening and mechanistic studies of viral RdRp activity.

microbiology↗

High-throughput super-resolution analysis of influenza virus pleomorphism reveals insights into viral spatial organization

Many viruses form highly pleomorphic particles; in influenza, these particles range from spheres of ~ 100 nm in diameter to filaments of several microns in length. Virion structure is of interest, not only in the context of virus assembly, but also because pleomorphic variations may correlate with infectivity and pathogenicity. We have used fluorescence super-resolution microscopy combined with a rapid automated analysis pipeline to image many thousands of individual influenza virions, gaining information on their size, morphology and the distribution of membrane-embedded and internal proteins. We observed broad phenotypic variability in filament size, and Fourier transform analysis of super resolution images demonstrated no generalized common spatial frequency patterning of HA or NA on the virion surface, suggesting a model of virus particle assembly where the release of progeny filaments from cells occurs in a stochastic way. Finally, we showed that in long filaments, viral RNP complexes are located preferentially within Archetti bodies, suggesting that these structures may play a role in virus transmission. Our approach therefore offers exciting new insights into influenza virus morphology and represents a powerful technique that is easily extendable to the study of pleomorphism in other pathogenic viruses.

microbiology↗

Rapid functionalisation and detection of viruses via a novel Ca2+-mediated virus-DNA interaction

Current virus detection methods often take significant time or can be limited in sensitivity and specificity. The increasing frequency and magnitude of viral outbreaks in recent decades has resulted in an urgent need for diagnostic methods that are facile, sensitive, rapid and inexpensive. Here, we describe and characterise a novel, calcium-mediated interaction of the surface of enveloped viruses with DNA, that can be used for the functionalisation of intact virus particles via chemical groups attached to the DNA. Using DNA modified with fluorophores, we have demonstrated the rapid and sensitive labelling and detection of influenza and other viruses using single-particle tracking and particle-size determination. With this method, we have detected clinical isolates of influenza in just one minute, significantly faster than existing rapid diagnostic tests. This powerful technique is easily extendable to a wide range of other enveloped pathogenic viruses and holds significant promise as a future diagnostic tool.

microbiology↗

Real-time analysis of single influenza virus replication complexes reveals large promoter-dependent differences in initiation dynamics

The viral RNA (vRNA) genome of influenza viruses is replicated by the RNA-dependent RNA polymerase (RNAP) via a complementary RNA (cRNA) intermediate. The vRNA promoter can adopt multiple conformations when bound by the RNAP. However, the dynamics, determinants, and biological role of these conformations are unknown; further, little is known about cRNA promoter conformations. To probe the RNA conformations adopted during initial replication, we monitored single, surface-immobilised vRNA and cRNA initiation complexes in real-time. Our results show that, while the 3 terminus of the vRNA promoter exists in dynamic equilibrium between pre-initiation and initiation conformations, the cRNA promoter exhibited very limited dynamics. Two residues in the proximal 3 region of the cRNA promoter (residues absent in the vRNA promoter) allowed the cRNA template strand to reach further into the active site, limiting promoter dynamics. Our results highlight promoter-dependent differences in influenza initiation mechanisms, and advance our understanding of virus replication.

microbiology↗