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.
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http://dx.doi.org/10.1099/jmm.0.000297 | DOI Listing |
Int J Mol Sci
December 2024
Digital Omics Research Center, Korea Basic Science Institute, Ochang 28119, Republic of Korea.
The COVID-19 pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has resulted in hundreds of millions of infections and millions of deaths globally. Although vaccination campaigns are mitigating the pandemic, emerging viral variants continue to pose challenges. The spike (S) protein of SARS-CoV-2 plays a critical role in viral entry by binding to the angiotensin-converting enzyme 2 (ACE2) receptor, making both proteins essential targets for therapeutic and vaccine development.
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March 2025
Melbourne Dental School, Bio21 Institute, The University of Melbourne, Parkville, Victoria, Australia. Electronic address:
The oral pathogen, Porphyromonas gingivalis has a general O-glycosylation system which it utilises to modify hundreds of proteins localised outside of the cytoplasm. The O-glycan is a heptasaccharide that includes a putative L-fucose and N-acetylgalactosamine (GalNAc) as the 5th and 6th sugar residues respectively. The putative L-fucose is expected to be synthesized as GDP-L-fucose involving the enzymes Gmd (PGN_1078) and Fcl (PGN_1079), while GalNAc is putatively epimerised from GlcNAc by GalE (PGN_1614).
View Article and Find Full Text PDFCarbohydr Res
February 2025
Department of Chemistry, Southern Illinois University Edwardsville, Edwardsville, IL, 62026, USA. Electronic address:
With the expanding use of phosphates as leaving groups in sialylations, little remains known about the C-5 effect towards their reactivity and stereoselectivity in the presence of a range of acceptors, and in different solvents. Herein we report the comparison between sialyl phosphate donors bearing N-acetyloxazolidinone and trifluoroacetamido functionalities at C-5. Excellent results and complete stereoselectivity were observed in several sialylations, but the outcome was influenced by the nature of the solvent and/or glycosyl acceptor.
View Article and Find Full Text PDFbioRxiv
December 2024
Graduate Field of Biophysics, Cornell University, Ithaca, NY, USA.
The abnormally thick glycocalyx of cancer cells can provide a physical barrier to immune cell recognition and effective immunotherapy. Here, we demonstrate an optical method based on Scanning Angle Interference Microscopy (SAIM) for the screening of therapeutic agents that can disrupt the glycocalyx layer as a strategy to improve anti-cancer immune responses. We developed a new membrane labeling strategy utilizing leucine zipper pairs to fluorescently mark the glycocalyx layer boundary for precise and robust measurement of glycocalyx thickness with SAIM.
View Article and Find Full Text PDFBiochim Biophys Acta Rev Cancer
December 2024
Department of Cell Biology, School of Life Sciences, Central South University, Changsha, Hunan 410013, PR China. Electronic address:
Liquid-Liquid Phase Separation (LLPS) is an important mechanism for the formation of functional droplets. Protein modification is an important pathway to regulate LLPS, in which series of modifying groups realize dynamic regulation by changing the charge and spatial resistance of the modified proteins. Meanwhile, uncontrolled protein modifications associated with LLPS dysregulation are highly correlated with tumorigenesis and development, suggesting the existence of a potential regulatory axis between the three.
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