Human parainfluenza viruses (HPIVs) are negative single-stranded RNA viruses belonging to the family Paramyxoviridae. HPIVs cause a spectrum of mild to severe respiratory symptoms predominantly in young children, transplant patients, immunocompromised individuals, and the elderly. Haemagglutinin-neuraminidase (HN) is one of two HPIV surface proteins with multiple roles in the viral lifecycle which make it an interesting target for structure-based drug designs. Although there are currently no licensed HPIV-specific antivirals to treat infected individuals, better understanding of HPIV infection mechanisms is essential to decrease the socioeconomic burden of HPIV diseases through drug and vaccine development. The prototype Human Parainfluenza Virus Type 3 (HPIV3) strain [HPIV3 Washington/1957 strain C243 (ATCC® VR-93™, referred to as HPIV3 C243)], was discovered in the late 1950s and has been propagated continuously in culture resulting in genetic and biological features that are not completely representative of currently circulating viral strains. Moreover, the host cell surface receptors that HPIV3 HN interacts with are not well understood and very few studies have explored the interactions between HPIV3 and glycans. We received an HPIV3 clinical isolate (referred to as HPIV3 CI) that was recovered from a hospitalised patient at Gold Coast University Hospital (Griffith University, Queensland, Australia) in 2016. Thus, the overall aim of this Thesis was to evaluate the genetic and biological features of the recently circulating HPIV3 CI compared to the prototype strain; and to characterise the glycan interactions of HPIV3.