Currently, COVID-19 has been reported in nearly all countries globally. To date, little is known about the viral shedding duration, clinical course and treatment efficacy of COVID-19 near Hubei Province, China. This multicentre, retrospective study was performed in 12 hospitals in Henan and Shaanxi Provinces from 20 January to 8 February 2020. Clinical outcomes were followed up until 26 March 2020. The viral shedding duration, full clinical course and treatment efficacy were analysed in different subgroups of patients. A total of 149 COVID-19 patients were enrolled. The median age was 42 years, and 61.1% (91) were males. Of them, 133 (89.3%) had fever, 131 of 144 (91%) had pneumonia, 27 (18.1%) required intensive care unit (ICU) management, 3 (2%) were pregnant, and 3 (2%) died. Two premature newborns were negative for SARS-CoV-2. In total, the median SARS-CoV-2 shedding period and clinical course

Human immunodeficiency virus type 1 (HIV-1) infection remains a severe public health problem worldwide. In this study, we investigated the distribution of HIV-1 subtypes and the prevalence of drug resistance mutations (DRMs) among patients with HIV-1 infection in Henan Province, China. HIV-1 strains in blood samples taken from inpatients and outpatients visiting the Sixth People's Hospital of Zhengzhou from August 2017 to July 2019 with a viral load (VL) greater than 1000 copies/ ml were subjected to subtype and DRMs analysis. Out of a total of 769 samples, subtype and DRM data were obtained from 657 (85.43%) samples. Phylogenetic analysis based on partial pol gene sequences indicated that the most commonly found genotype was subtype B (45.51%, 299/657), followed by CRF01_AE (28.61%, 188/657), CRF07_BC (15.68%, 103/657), CRF08_BC (0.76%, 5/657), C (0.61%, 4/657), A (0.30%, 2/657), and others (8.52%, 56/657). Circulating recombinant forms (CRFs) were most commonly found in patients who were naïve to antiretroviral treatment (ART) (68.67%, 160/233). The percentage of patients with one or more major drug-resistance mutations was 50.99% (335/657), and it was 6.44% (15/233) in ART-naive patients that were primarily infected with subtype B (17.74%). Resistance mutations were most common at codons 65, 103, 106, 184, and 190 of the reverse transcriptase gene and codon 46 of the protease gene. Our study provides detailed information about the distribution of HIV-1 subtypes and the incidence of drug resistance mutations of different subtypes in ART-experienced and naïve patients. This can guide policymakers in making decisions about treatment strategies against HIV-1.

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GII.3 and GII.6 noroviruses (NoVs) are similar in several aspects, including the presence of a short sequence insertion in the P2 domain of the major capsid protein (VP1) and trypsin susceptibility of VP1-containing virus-like particles (VLPs). In this study, we generated two constructs with the S or P domains of VP1 from GII.3 and GII.6 NoV strains exchanged (GII.3S/GII.6P and GII.6S/GII.3P), and the resultant chimeric capsid proteins were expressed from recombinant baculoviruses. The assembly of VLPs was confirmed by electron microscopy, and the susceptibility of assembled VLPs to trypsin digestion was analyzed by SDS-PAGE. Salivary histo-blood group antigen (HBGA) binding and binding blockade assays were performed to determine the binding characteristics of chimeric VP1-containing VLPs with and without trypsin digestion. Our results indicated that both expressed GII.3S/GII.6P and GII.6S/GII.3P chimeric proteins successfully assembled into VLPs. Trypsin digestion of VLPs assembled from both chimeric proteins led to the generation of two fragments with molecular sizes similar to those of wild-type VP1-containing VLPs. An in vitro salivary HBGA binding assay demonstrated that VLPs assembled from both chimeric proteins exhibited enhanced binding after trypsin cleavage. An HBGA binding blockade assay indicated that the binding of GII.3S/GII.6P and GII.6S/GII.3P VLPs against salivary HBGAs could only be blocked by GII.3 and GII.6 NoV VLP-specific hyperimmune sera, respectively. For GII.6 and GII.3S/GII.6P VLPs, a difference in binding enhancement after trypsin cleavage was observed. Our results demonstrate that the S domains of GII.3 and GII.6 NoV VP1 are interchangeable and that the S domain affects the binding of the P domain to HBGAs.