Ask about this productRelated genes to: RPSA antibody
- Gene:
- RPSA NIH gene
- Name:
- ribosomal protein SA
- Previous symbol:
- LAMR1
- Synonyms:
- LRP, 37LRP, p40, SA
- Chromosome:
- 3p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1992-06-03
- Date modifiied:
- 2019-04-23
Related products to: RPSA antibody
Related articles to: RPSA antibody
- To investigate the effects of mutations on pyrazinamide (PZA)-associated regions, including , , , and , among multidrug-resistant tuberculosis (MDR-TB) isolates from China. A total of 139 MDR-TB isolates from China underwent PZA susceptibility testing and genotyping, and the sequences of the four PZA resistance-associated regions were analyzed. The association between lineage and PZA resistance was analyzed, as well as that between lineage and mutation. Among 139 MDR-TB isolates, 62 were resistant to PZA. Of these 62 PZA-resistant isolates, 60 harbored at least one nonsynonymous mutation in the , , or . None of the isolates contained a mutation in . Most mutations in PZA-resistant isolates were concentrated in , while mutations in other genes were rare and usually accompanied by mutations in . The single mutation outside observed in a PZA-resistant isolate was a novel mutation G(-131)A. The mutation Pro796Leu in was exclusively detected in lineage 4 strains and correlated with this lineage, but was not associated with PZA resistance. The DNA sequencing of proved to be the most effective approach for detecting PZA resistance, with an accuracy of 92.81%. Notably, some PZA-susceptible isolates still carried mutations in , , or . This study highlights the complexity of PZA resistance. These findings expand our understanding of the molecular features associated with PZA resistance in China. - Source: PubMed
Publication date: 2026/05/20
Bo Xiang-LongLi Ma-ChaoHang HaoLin Shi-QiangLiu Hai-CanQian ChengLi Gui-LianZhao Xiu-QinWan Kang-LinZhao Li-Li - Sodium azide inhibits bacterial growth by inhibiting the SecA-dependent translocation of proteins across the cytoplasmic membrane, and all of the mutations known to confer increased resistance to azide are in the gene. However, the molecular mechanism of resistance is unclear. To gain insight into this mechanism, we designed a genetic screen to isolate transposon insertion mutations that conferred increased resistance to sodium azide, which were also unlinked to . We isolated six mutants, which we dubbed mutants, containing insertions in the , , and genes. Growth of in the presence of azide causes increased accumulation of the larger of two previously noted, but uncharacterized, isoforms of SecA. However, the mutations caused increased production of the smaller isoform in the presence of azide. Mutations in the gene that confer azide resistance also caused increased production of the small SecA isoform in the presence of azide, suggesting a shared mechanism. Expression of truncated variants of SecA, which lack the C-terminal tail, caused moderately increased resistance to azide, and Western blotting analysis confirmed that the smaller SecA isoform lacks the C-terminal ~70 amino acids. These results indicate that produces two SecA isoforms under normal growth conditions and that changes in the proportions of the isoform correlate with resistance to sodium azide. - Source: PubMed
Jiang ChenMilner MathewWilliams GeorgiaAbdullah OsamaLund PeterHuber Damon - Pseudomonas aeruginosa biofilms drive chronic infections, yet heterogeneous matrix composition hinders standardized in vitro classification of clinical isolates. This study aimed to develop a reproducible biofilm formation protocol using a defined supplement mix and elucidate proteomic signatures across biofilm categories to enable risk stratification and targeted therapies. - Source: PubMed
Publication date: 2026/05/08
Rain ZinnuSingh Ashish KumarKumari ShabnamKumar DeepakMaurya Ganesh KumarKumar RajneeshPrakash Pradyot - African swine fever virus (ASFV) poses a severe threat to the global pig industry, yet the precise mechanisms of its entry into host cells are not fully understood. In this study, we identified the host ribosomal protein SA (RPSA), a protein located in lipid rafts, as a critical viral receptor that facilitates ASFV entry. Immunoprecipitation-mass spectrometry (IP-MS) screening results identified RPSA as a binding partner of the ASFV capsid protein pE120R, which was further confirmed by co-immunoprecipitation (Co-IP) and immunofluorescence assays (IFA) in ASFV-infected cells. Moreover, knockdown of RPSA expression in porcine alveolar macrophages (PAMs) by siRNA significantly reduced ASFV attachment and internalization. In contrast, ectopic overexpression of RPSA in permissive CV-1 cells enhanced the attachment and internalization of ASFV virions. Additionally, we observed that both pharmacological inhibition of caveola-mediated endocytosis (CavME) with nystatin and genetic knockdown of caveolin-1 (CAV1) decreased caveola-mediated ASFV virions endocytosis and internalization. Mechanistically, RPSA interacts with CAV1, a major structural protein of caveolae. Domain mapping showed that pE120R mainly binds to the LR2 and LR3 domains of RPSA, while RPSA interacts with CAV1 via its 16B domain, forming a pE120R-RPSA-CAV1 complex that facilitates ASFV entry. Overall, these results demonstrate that RPSA works as a potential host receptor linking ASFV pE120R to the CAV1-mediated endocytic pathway, facilitating viral entry through caveola-mediated endocytosis. These findings advance our understanding of ASFV entry mechanism and offer a potential target for antiviral strategies against ASFV. - Source: PubMed
Publication date: 2026/05/11
Liu ChuanxiaLi TingtingWang YibingZhao FeiLi JiangnanHuang LiWeng Changjiang - Neutrophil migration to bacterial infection sites is key for host defense. Host ribosomal protein SA (RPSA) has been recently reported to regulate the anti-infection immunity of immune cells; however, its role in neutrophil migration remains unclear. Here, using myeloid-specific Rpsa-deficient mice, we found that RPSA deletion inhibited neutrophil infiltration and markedly exacerbated Streptococcus suis serotype 2 infection. Adoptive cell transfer and neutrophil depletion assays identified RPSA as vital for the anti-infective function of neutrophils. Mechanistically, RPSA deficiency induced the overexpression of olfactomedin 4 (OLFM4), which in turn inhibited the activation of the RhoA/ROCK1/pMLC2 signaling pathway, reduced MYH9 expression, and caused aberrant MYH9 translocation from the uropod to the cytosol in migrating neutrophils. Ultimately, this disrupted cytoskeletal polarization and uropod extension, thereby abrogating migratory function. Clinically, septic patients' neutrophils exhibited reduced RPSA and elevated OLFM4 expression, a phenotype that correlated with a marked impairment of migratory capacity. Therapeutic targeting of the RPSA-OLFM4 axis restored neutrophil migration and improved disease outcomes in both S. suis 2-infected and septic mice. Thus, our findings demonstrate that RPSA promotes neutrophil migration via downregulating OLFM4 to counter bacterial infection, and establish the RPSA-OLFM4 axis as a critical immune migratory checkpoint in host antibacterial immunity. - Source: PubMed
Publication date: 2026/04/25
Wu TongYang XiangruiLei SiyuWei ShaopengWang WeiSun YiJiang HexiangJia XiuwenTian YanyanZhang KaixinZhang YufanChen HaizhenHuang JingLi FengyangLi NaLei Liancheng