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Porcine reproductive and respiratory syndrome virus (PRRSV) critically threatens the pig industry in China. Lineage 1 PRRSV, which is divided into L1A–L1F and L1H–L1J, is widely recognized as the most extensively genetically diverse lineage globally. L1A (NADC34-like) and L1C (NADC30-like) PRRSVs have become the current major circulating strains in China. Notably, strains from other branches of L1 have not been reported in China. During our epidemiological investigation of PRRSV, we identified a new strain named HLJDZD55. Phylogenetic analysis of the ORF5 gene revealed that HLJDZD55 belongs to the L1B branch. Alignment of deduced amino acid sequences based on the Nsp2 gene indicated that HLJDZD55 has a discontinuous deletion of 131 amino acids (111 + 1 + 19). We further sequenced the whole genome of HLJDZD55, and phylogenetic analysis based on the whole-genome sequence revealed that HLJDZD55 belongs to the L1C branch. Recombination analysis of the whole genome demonstrated that HLJDZD55 is a recombinant strain of TJZH-1607 (L1C, identified in China) and Minnesota 14 (L1B, identified in the USA). These findings suggested that HLJDZD55 is a newly emerged lineage 1 PRRSV in China and is closely related to L1B PRRSV in the US, which may have been introduced from the U.S. strain and subsequently recombined with the local Chinese strain and underwent evolution. Taken together, these results demonstrated the emergence of L1B PRRSV in China for the first time. [ABSTRACT FROM AUTHOR]

Simple Summary: We conducted a study on flightin, a vital protein found in insect flight muscles, with a specific focus on the social wasp Vespa basalis, which is a dangerous hornet species. Using sequence analysis techniques, we successfully obtained an 1189 bp cDNA sequence encoding the flightin protein consisting of 150 amino acids. According to our analysis, the molecular weight and isoelectric point of the amino acid sequence are 18.05 kDa and 5.84, respectively. The protein lacks a transmembrane topology structure, and we identified four patterns of functional sites. Conducting phylogenetic analysis on 38 species, including 8 Vespidae species, revealed a close evolutionary relationship between Vespa basalis and Vespa mandarinia. These findings warrant further investigation, especially considering the contrasting information obtained from the analysis of mitochondrial sequences. Flight is a complex physiological process requiring precise coordination of muscular contraction. A key protein in insect flight is flightin, which plays an integral role in the flight muscles. This research sought to evaluate the flight competence of the social wasp V. basalis by characterizing the molecular components involved. Our study focused on Vespa basalis, one of the most dangerous hornet species, utilizing PCR to obtain a partial cDNA sequence of the flightin protein. We then employed phylogenetic and sequence analysis to gain insights into this protein in flight-related adaptations. The cDNA has an 1189-base pair sequence including an open reading frame (453 bp) encoding 150 amino acids. Analyzing the deduced amino acid sequence using an online tool revealed a molecular weight of 18.05 kDa, an isoelectric point of 5.84, four functional site patterns, and no transmembrane topology. We constructed a phylogenetic tree of flightin based on 38 species. Our analysis indicated that V. basalis is most closely related to V. mandarinia; this alignment is consistent with their similar aggressive behavior, but their evolutionary relationship, based on mitochondrial sequences, presents a contrast. These initial findings on the flightin gene in V. basalis lay the groundwork for future functional studies to elucidate its specific role in flight adaptations and explore its potential as a target for pest management strategies. [ABSTRACT FROM AUTHOR]