Thaumetopoea pityocampa (pine processionary moth) is one of the most important pine pests in the forests of Mediterranean countries, Central Europe, the Middle East and North Africa. Apart from causing significant damage to pinewoods, T. pityocampa occurrence is also an issue for public and animal health, as it is responsible for dermatological reactions in humans and animals by contact with its irritating hairs. High throughput sequencing technologies have allowed the fast and cost-effective generation of genetic information of interest to understand different biological aspects of non-model organisms as well as the identification of potential pathogens. Using these technologies, we have obtained and characterized the transcriptome of T. pityocampa larvae collected in 12 different geographical locations in Turkey. cDNA libraries for Illumina sequencing were prepared from four larval tissues, head, gut, fat body and integument. By pooling the sequences from Illumina platform with those previously published using the Roche 454-FLX and Sanger methods we generated the largest reference transcriptome of T. pityocampa. In addition, this study has also allowed identification of possible viral pathogens with potential application in future biocontrol strategies.

The envelope (env) protein of SARS-CoV-2, a pivotal component of the viral architecture, plays a multifaceted role in viral assembly, replication, pathogenesis, and ion channel activity. These features make it a significant target for understanding virus–host interactions and developing vaccines to combat COVID-19. Recent structural studies provide valuable insights into the conformational dynamics and membrane topology of the SARS-CoV-2 env protein, shedding light on its functional mechanisms. The strong homology and highly conserved structure of the SARS-CoV-2 env protein shape its immunogenicity and functional characteristics. This study examines the ability of the recombinant SARS-CoV-2 env protein to stimulate an immune response. In this study, recombinant envelope proteins were produced using the baculovirus expression system, and their potential efficacy was evaluated in both in vivo and in vitro models. Our results reveal that the env protein of SARS-CoV-2 stimulates humoral and cellular responses and highlight its potential as a promising vaccine candidate for combating the ongoing pandemic.

The Amsacta moorei entomopoxvirus (AMEV) belongs to the Entomopoxvirinae subfamily of poxviruses. Although entomopoxviruses are very similar to poxviruses of humans, they have no potential risk for humans because they only infect insects. Intensive studies have been carried out on this virus because it can potentially be used as gene therapy and gene expression vectors. The AMEV genome has 256 open reading frames and two of them, AMV153 and AMV197, are putative protein kinases. Protein kinases of some vertebrate poxviruses have some functions in virus morphogenesis, regulation of the cell cycle, and apoptosis of the host. In previous studies, the molecular structure of AMV197 protein kinase was elucidated, its transcriptomic properties in cell culture and its function in progeny virus production were determined, and an AMV197-defective virus (AmΔPK/gfp) was produced. However, the function of AMV153 in this scenario remained as unclear, and it is crucial to know its function to better understand the role of protein kinases in the replication of AMEV. The AMV153 was first deleted from the genome of AmΔPK/gfp and subsequently from the genome of AMEV, creating two separate recombinant viruses. The homologous recombination method was used to replace AMV153 ORF with mCherry gene that produces red fluorescent protein. Mutant viruses in which the AMV153 gene was replaced with mCherry were identified by fluorescence microscopy but could not be propagated separately from the AmΔPK/gfp or wild-type viruses in insect cells. Unsuccessful attempts to isolate the mutant viruses with the AMV153 gene deletion first in AmΔPK/gfp virus and second in wild type AMEV structure, suggested that the protein kinase encoded by AMV197 cannot substitute the function of AMV153 and the AMV153 protein is essential for virus replication.