The coronaviruses (CoVs), which are a family of positive-strand RNA viruses, infect the mammals and birds. Seven CoVs are responsible for human-to-human transmission, especially the SARS-CoV-2, thereby posing a daunting challenge to global public health security. As the most common modification in viral glycoproteins, glycosylation plays the crucial role in host recognition, immunity avoidance, virus replication, assembly and transmission. In this review, we summarized and discussed the latest studies about glycosylation in coronaviridae members. Focused on the spike protein, nearly one hundred of N/O-glycosyltion sites have been reported. The N-glycans from spike protein are dominated by the high-mannose and complex-type, while the O-glycosylation is rather complicated. Significantly, it is known that the viral glycosylation depend on host cells, thus the glycan pattern of the produced recombinant viral glycoproteins might be different from that of native viral proteins, which represent a crucial determinant for vaccine design. The latest results based on bioinformatics, biochip, mass spectrography and genetic technology facilitate the overall perspective for glycosylation researching in CoVs. By summarizing the distribution of glycosylation sites, the structure of glycans, the biological functions and the research technologies, this review will help promote diagnosis, treatment and vaccine development related to coronaviruses.