As a disease with unknow etiology, the use of autoantibodies as biomarkers for the early detection of systemic lupus erythematosus(SLE) is associated with a high false-positive rate, suggesting changes in antibody characteristics during disease progression. N-glycosylation is a critical post-translational modification of antibodies that significantly influences their structure and receptor binding modulation, thereby altering the elicited biological activities and functions. Numerous studies have analyzed the impact of monosaccharides, such as sialic acid, fucose, and N-acetylglucosamine, which constitute N-glycans, on the immunological functions of antibodies. This review systematically summarized the aberrant immunoglobulin G (IgG) N-glycosylation patterns identified in SLE patients, with emphasis on the correlations between disease progression/complications and quantitative alterations of individual glycan components. Addressing the weaknesses, contradictions, and gaps in current research, we analyzed the limitations of existing methodologies and discussed the potential solution for resolving these issues, thereby providing direction for the development of subsequent glycomics analysis methods. Finally, considering the close relationship between antibody glycosylation modifications and SLE, this paper introduced high-resolution clinical diagnostic and monitoring approaches, as well as low-cost and hypoallergenic therapeutic strategies based on glycan biology. In summary, abnormal glycosylation occurred during the onset and progression of SLE, which had been clearly observed on the basis of advanced glycomics techniques, and thus promoting progress in clinical diagnosis and treatment strategies.