@article{mbs:/content/journal/jmm/10.1099/jmm.0.000297, author = "Košutić-Gulija, Tanja and Slovic, Anamarija and Ljubin-Sternak, Sunčanica and Mlinarić-Galinović, Gordana and Forčić, Dubravko", title = "A study of genetic variability of human parainfluenza virus type 1 in Croatia, 2011–2014", journal= "Journal of Medical Microbiology", year = "2016", volume = "65", number = "8", pages = "793-803", doi = "https://doi.org/10.1099/jmm.0.000297", url = "https://www.microbiologyresearch.org/content/journal/jmm/10.1099/jmm.0.000297", publisher = "Microbiology Society", issn = "1473-5644", type = "Journal Article", keywords = "haemagglutinin-neuraminidase", keywords = "phosphoprotein", keywords = "HPIV1", keywords = "fusion protein", keywords = "molecular epidemiology", abstract = "Molecular epidemiology of human parainfluenza viruses type 1 (HPIV1) was investigated. Samples were collected from patients hospitalized in Croatia during the three consecutive epidemic seasons (2011–2014). Results indicated co-circulation of two major genetic clusters of HPIV1. Samples from the current study refer to clades II and III in a phylogenetic tree of haemagglutinin–neuraminidase (HN) gene. Additional phylogenetic trees of fusion (F) and phosphoprotein (P) genes confirmed the topology. Analysis of nucleotide diversity of entire P, F and HN genes demonstrated similar values: 0.0255, 0.0236 and 0.0237, respectively. However, amino acid diversity showed F protein to be the most conserved, while P protein was the most tolerant to mutations. Potential N- and O-glycosylation sites suggested that HPIV1 HN protein is abundantly glycosylated, and a specific N-glycosylation pattern could distinguish between clades II and III. Analysis of potential O-glycosylation sites in F protein indicated that samples from this study have two potential O-glycosylation sites, while publicly available sequences have five potential sites. This study provides data on the molecular characterization and epidemic pattern of HPIV1 in Croatia.", }