Feline panleukopenia (FPL) is a highly contagious infectious disease caused by infection with feline parvovirus (FPV) and canine parvovirus type 2 (CPV‐2). In recent years, the number of cats with FPL has increased with the expansion of pet cat population in China. The feces of 51 cats with diarrhea symptoms collected from 2021 to 2022 in Eastern Shandong, China, were detected by polymerase chain reaction for parvovirus and other viruses related to feline diarrhea to investigate the prevalence and gene variation of parvovirus in cats. In all the 51 samples, 45.1% (23/51) were positive for at least one viral pathogen, and the positivity of parvovirus was 41.2% (21/51), showing a high prevalence. Multiple‐pathogen testing indicated high‐coinfection rates of 42.9% (9/21) with other common viruses in parvovirus‐positive cats. Most of the coinfections are feline coronavirus (FCoV), followed by feline astrovirus (FAstV) and feline bocavirus (FBoV). The complete VP2 sequences of 21 parvoviruses were obtained. Among them, 20 sequences were identified as FPV, and only one was CPV‐2c of Asian origin, which was first detected from cats in Eastern Shandong, China. A phylogenetic tree of the 20 FPVs was constructed together with 698 FPVs (cat/dog host) worldwide on the basis of complete VP2. The 18 FPVs displayed high‐sequence identity to one another (99.8%–100%), and they were clustered into FPV‐G1 group, whereas the other two were clustered into FPV‐G3 group. The FPV‐G1 group increased dramatically to become predominant after 2019 in China, contributing to the prevalence of A91S mutation due to 96.07% FPV‐G1 with A91S mutation as well as 100% of FPV‐G2 and 99.12% of FPV‐G3 with 91A in the statistical analysis. This study enriched the understanding of the prevalence, molecular evolution, and cross‐species transmission of parvovirus in cats and provided a basis for responding to challenges in the diagnosis and treatment of FPL.

Canine distemper virus (CDV) infects many sensitive species worldwide and its host range is expanding. The hemagglutinin (H) protein, the major neutralizing target, binds to cellular receptors and subsequently triggers fusion for initial viral infection. So it’s necessary to clarify the precise neutralizing epitopes of H protein and extend the knowledge of mechanisms of virus neutralization. In this study, a neutralizing monoclonal antibody (mAb) 2D12 against CDV H protein, which had different reactivity with different CDV strains, was generated and characterized. A series of truncated H proteins were screened to define the minimal linear epitope 238DIEREFD244 recognized by 2D12. Further investigation revealed that the epitope was highly conserved in America-1 vaccine lineage of CDV strains, but different substitutions in the epitope appeared in CDV strains of the other lineages and two substitutions (D238Y and R241G) caused the change of antigenicity. Thus, the epitope represents a novel lineage-specific neutralizing target on H protein of CDV for differentiation of America-1 vaccine lineage and the other lineages of CDV strains. The epitope was identified to localize at the surface of H protein in two different positions in a three-dimensional (3D) structure, but not at the position of the receptor-binding site (RBS), so the mAb 2D12 that recognized the epitope did not inhibit binding of H protein to the receptor. But mAb 2D12 interfered with the H-F interaction for inhibiting membrane fusion, suggesting that the mAb plays key roles for formation of H-F protein oligomeric structure. Our data will contribute to the understanding of the structure, function, and antigenicity of CDV H protein and mechanisms of virus neutralization.