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Martin, K. M.

Publications and source records attributed to Martin, K. M..

6 recordsLinked to original sources

Virome of Culex nigripalpus at an Alabama aquaculture site reveals diverse insect-specific viruses and the impact of dual bioinformatic pipelines

Mosquitoes are important cosmopolitan insect vectors that threaten humans and host a variety of diseases. Catfish production from Alabama fisheries supports the development of favorable habitats that benefit fish, birds, and insects. Our study found that Culex nigripalpus was a major vector associated with catfish ponds. As Culex nigripalpus harbors medically important viruses like St. Louis encephalitis, studies often focus on these without exploring the full virus diversity. To address this, we performed an RNA-Seq analysis on Culex nigripalpus and compared bioinformatic methodologies, testing two approaches. In the first method (reference-based assembly), the characterized genome of Culex quinquefasciatus was used with a mapping cutoff, and assembled contigs were annotated with megablast against the NCBI nucleotide database. In a second method, reads were assembled de novo, and the contigs were annotated with a BLAST against the NCBI viral genomic database. In addition, the cross-validation of the contigs generated by the two methods was conducted to identify the common and unique viral contigs, adding support for identification. RNA-Seq analysis identified fifteen different viruses. Both methods identified three common viruses, Merida virus isolate Cx. nigripalpus1 (PQ963471), Hubei mosquito virus 5 isolate Cx. nigripalpus2 (PQ963472), and Zhejiang mosquito virus isolate Cx. nigripalpus3 (PQ963484). The first method also identified ten unique viruses, and the second method generated two unique viruses. Selected viruses were independently validated by RT-PCR amplification of viral genomic regions. Overall, our data suggest that different approaches to bioinformatic analysis complement each other and improve viral genome recovery from metatranscriptomic datasets.

microbiology↗

Characterization of Soybean Vein Necrosis Virus (SVNV) Proteins: Sequence Analysis of Field Strains and Comparison of Localization Patterns in Differing Cell Types

Soybean vein necrosis virus (SVNV) is a persistent, propagative, ambisense-ssRNA virus in the genus Orthotospovirus transmitted by Nehydratothrips variabilis. In this study, five open reading frames (ORFs) (N, NSs, NSm, GN, and GC) were fused in frame to GFP for use in both plant and insect cells. N and NSs localize in plants to the cell periphery and nucleus. NSm causes cell death to plant cells but not in insect cells where cytoplasmic localization is seen. GN and GC glycoproteins localize to the membranes and accumulate with more cytoplasmic localization seen in insect cells. To understand SVNV in the field, we collected 33 samples expressing symptoms of SVNV. The N, NSs, and NSm ORFs were sequenced and amino acid mutations in each gene were seen. The findings of this study capture sequence changes which have occurred over the past fifteen years compared to the localization of proteins never before conducted.

pathology↗

Visualizing tomato spotted wilt virus protein localization: Cross-kingdom comparisons of protein-protein interactions.

Tomato spotted wilt virus (TSWV) is an orthotospovirus that infects both plant and insect cells. Understanding the protein localization and interactions in these cells is crucial for unraveling the infection cycle and host-virus interactions. In this study, we investigated the localization of TSWV proteins in cells of plants and insects. Furthermore, we identified the protein-protein interactions among TSWV proteins using bimolecular fluorescence complementation (BiFC) and yeast two-hybrid (MbY2H) assays. Our results revealed distinct localization patterns for TSWV proteins in plant and insect cells. The nucleocapsid protein (N), essential for genome encapsidation, was found in the cytoplasm of both cell types. The non-structural movement protein (NSm) localized to the cytoplasm in insect cells, different from the localization in plant cells plasmodesmata. The non-structural silencing protein (NSs) exhibited peripheral localization in plant cells and cytoplasmic localization in insect cells. Additionally, glycoproteins GN and GC showed cytoplasmic localization in both cell types. Moreover, protein-protein interaction analyses revealed self-interactions of NSm, N, GN, GC, and NSs. These interactions are crucial for viral genome encapsidation, virion assembly, and RNA silencing suppression. We also identified interactions between different TSWV proteins, indicating their roles and host interactions. Comparisons with other orthotospovirus interaction maps highlighted the uniqueness of TSWV protein-protein interaction networks. Despite sharing genome organization and putative gene annotations, each orthotospovirus exhibited distinct interaction maps. Overall, this research expands our knowledge of TSWV infection and elaborates on the intricate relationships between viral proteins, cellular dynamics, and host responses. These findings lay the groundwork for future studies on the molecular mechanisms of TSWV infection and may facilitate the development of effective control strategies.

cell biology↗

Rescue of the first Alphanucleorhabdovirus entirely from cloned complementary DNA: an efficient vector for systemic expression of foreign genes in maize and insect vectors.

Recent reverse genetics technologies have enabled genetic manipulation of plant negative-strand RNA virus (NSR) genomes. Here, we report construction of an infectious clone for the maize-infecting Alphanucleorhabdovirus maydis, the first efficient NSR vector for maize. The full-length infectious clone was established using agrobacterium-mediated delivery of full-length maize mosaic virus (MMV) antigenomic RNA and the viral core proteins (nucleoprotein N, phosphoprotein P, and RNA-directed RNA polymerase L) required for viral transcription and replication into Nicotiana benthamiana. Insertion of intron 2 ST-LS1 into the viral L gene increased stability of the infectious clone in Escherichia coli and Agrobacterium tumefaciens. To monitor virus infection in vivo, a GFP gene was inserted in between the N and P gene junctions to generate recombinant MMV-GFP. cDNA clones of MMV-WT and MMV-GFP replicated in single cells of agroinfiltrated N. benthamiana. Uniform systemic infection and high GFP expression were observed in maize inoculated with extracts of the infiltrated N. benthamiana leaves. Insect vectors supported virus infection when inoculated via feeding on infected maize or microinjection. Both MMV-WT and MMV-GFP were efficiently transmitted to maize by planthopper vectors. The GFP reporter gene was stable in the virus genome and expression remained high over three cycles of transmission in plants and insects. The MMV infectious clone will be a versatile tool for expression of proteins of interest in maize and cross-kingdom studies of virus replication in plant and insect hosts.

plant biology↗

Identification of interacting proteins of maize mosaic virus glycoprotein in its vector, Peregrinus maidis.

Rhabdovirus glycoproteins (G) serve multifunctional roles in virus entry, assembly, and exit from animal cells. We hypothesize that maize mosaic virus (MMV) G is required for invasion, infection, and spread in Peregrinus maidis, the planthopper vector. Using a membrane-based yeast two-hybrid assay, we identified 125 P. maidis proteins that physically interacted with MMV G, of which 68% matched proteins with known functions in endocytosis, vesicle-mediated transport, protein synthesis and turnover, nuclear import/export, metabolism and host defense. Physical interaction networks among conserved proteins indicated a possible cellular coordination of processes associated with MMV G translation, protein folding and trafficking. Non-annotated proteins contained predicted functional sites, including a diverse array of ligand binding sites. Cyclophilin A and apolipophorin III co-immunoprecipitated with MMV G, and each showed different patterns of co-localization with G in insect cells. This study describes the first protein interactome for a rhabdovirus spike protein and insect vector.

microbiology↗

Discovery of novel thrips vector proteins that bind to the plant bunyavirus, tomato spotted wilt virus.

The plant-pathogenic virus, tomato spotted wilt virus (TSWV), encodes a structural glycoprotein (GN) that, like with other bunyavirus/vector interactions, serves a role in viral attachment and possibly entry into arthropod vector host cells. It is well documented that Frankliniella occidentalis is one of seven competent thrips vectors of TSWV transmission to plant hosts, however, the insect molecules that interact with viral proteins, such as GN, during infection and dissemination in thrips vector tissues are unknown. The goals of this project were to identify TSWV-interacting proteins (TIPs) that interact directly with TSWV GN and to localize expression of these proteins in relation to virus in thrips tissues of principle importance along the route of dissemination. We report here the identification of six TIPs from first instar larvae (L1), the most acquisition-efficient developmental stage of the thrips vector. Sequence analyses of these TIPs revealed homology to proteins associated with the infection cycle of other vector-borne viruses. Immunolocalization of the TIPs in L1s revealed robust expression in the midgut and salivary glands of F. occidentalis, the tissues most important during virus infection, replication and plant-inoculation. The TIPs and GN interactions were validated using protein-protein interaction assays. Two of the thrips proteins, endocuticle structural glycoprotein and cyclophilin, were found to be consistent interactors with GN. These newly discovered thrips protein-GN interactions are essential towards better understanding of transmission of persistent propagative plant viruses by their vectors, as well as for developing new strategies of insect pest management and virus resistance in plants.\n\nImportance StatementThrips-transmitted viruses cause devastating losses to numerous food crops worldwide. For negative-sense RNA viruses that infect plants, the arthropod serves as a host as well by supporting virus replication in specific tissues and organs of the vector. The goal of this work was to identify vector/host proteins that bind directly to the viral attachment protein and thus may play a role in the infection cycle in the insect. Using the model plant bunyavirus, tomato spotted wilt virus (TSWV), and the most efficient thrips vector, we identified and validated six TSWV-interacting proteins from Frankliniella occidentalis first instar larvae. Two proteins, an endocuticle structural glycoprotein and cyclophilin, were able to interact directly with the TSWV attachment protein, GN, in insect cells. The TSWV GN-interacting proteins provide new targets for disrupting the virus-vector interaction and could be putative determinants of vector competence.

microbiology↗