mouse integrin αvβ3  (R&D Systems)

Journal: Military Medical Research

Article Title: Octopus-inspired engineered bacteria with a plug-and-play surface display system achieves enhanced tumor-specific colonization and antitumor immunity

doi: 10.1016/j.mmr.2026.100030

Figure Lengend Snippet: Schematic of the construction and therapeutic mechanism of the octopus-inspired triple-engineered bacteria (OITE strain) . The antitumor attenuated Salmonella typhimurium AISI strain was triple-engineered. (1) ST/SC-RGD×4 “tentacles”-Surface modification: the ST sequence was expressed within the external third loop of OmpA in the AISI strain, resulting in the AISI-ST strain. The ST protein was coexpressed with OmpA (OmpA-ST fusion protein) localized to the bacterial outer membrane. An incubation with SC-RGD×4 protein (SC-RGD×4) led to the formation of AISI-ST/SC-RGD×4 strain (AISI-ST/SC-RGD×4) through ST-SC-mediated covalent conjugation. (2) Dynamic EPS “camouflage”-Immunoactivation engineering: the AISI-H-ST strain was created by introducing the quorum-sensing (QS) promoter pLuxI to control HtrA expression into AISI-ST strain, which specifically increased HtrA-mediated extracellular polysaccharide (EPS) production to amplify bacteria-mediated immune activation. (3) Anti-PD1nanobody (PD1nb) “secretion”-Checkpoint blockade engineering: further programming of AISI-H-ST strain enabled QS-triggered anti-PD1nb secretion, generating the AISI-HP-ST strain. The incubation of AISI-HP-ST strain with SC-RGD×4 protein finally produced the OITE strain (AISI-HP-ST/SC-RGD×4). The intravenously administered OITE strain highly selectively accumulates in tumors through RGD-αvβ3 integrin interactions, with subsequent bacterial proliferation initiating two therapeutic actions: HtrA-mediated immune activation via increasing immune cells infiltration and activation, and secreted PD1nb-based blockade of PD-1/PD-L1 immunosuppressive signaling. OITE. Octopus-inspired, triple-engineered bacterium; AISI. Attenuated Salmonella Δ htrA :: luxI - VNP20009 strains; ST. SpyTag; SC. SpyCatcherΔ; RGD. Arginine-glycine-aspartic acid; HtrA. High-temperature requirement A; PD1. Programmed cell death protein 1; H. HtrA; HP. HtrA and PD1nb; AHL. N-acyl homoserine lactone; MACS. Macrophages; Teffs. Effector T cells; Tregs. Regulatory T cells.

Article Snippet: To prepare the surfaces for the strain adhesion assays, the recombinant mouse integrin αvβ3 (TGAV & ITGB3) heterodimer protein (HY-P700761, MCE, USA) was first diluted to 10 μg/ml in 50 mmol/L carbonate buffer (pH 9.6).

Techniques: Bacteria, Modification, Sequencing, Membrane, Incubation, Conjugation Assay, Control, Expressing, Activation Assay, Produced

Journal: Oncology Letters

Article Title: Bone sialoprotein stimulates cancer cell adhesion through the RGD motif and the αvβ3 and αvβ5 integrin receptors

doi: 10.3892/ol.2024.14675

Figure Lengend Snippet: Effect of anti-αvβ3 or anti-αvβ5 antibody on cancer cell adhesion to BSP, as determined by the alamarBlue ® assay. (A) MDA-MB-231 (n=4), (B) PC-3 (n=4) and (C) NCI-H460 (n=4) cells were incubated for 60 min at 37°C in the presence of 10 µg/ml isotype control IgG1, 10 µg/ml anti-αvβ3 antibody or 10 µg/ml anti-αvβ5 antibody. Afterwards, cells were cultured for 2 h on BSP-coated plates and attached cells were examined. Data are reported as percentages compared with 10 µg/ml isotype control IgG1 (100%). Error bars represent the standard deviation. **P<0.01; ****P<0.0001 vs. negative control IgG1. BSP, bone sialoprotein; ns, not significant.

Article Snippet: Anti-integrin αvβ3 mouse monoclonal antibody, (clone LM609; catalogue no. MAB1976Z) and anti-integrin αvβ5 mouse monoclonal antibody (clone P1F6; catalogue no. MAB1961Z) were obtained from Millipore (Merck KGaA).

Techniques: Alamar Blue Assay, Incubation, Control, Cell Culture, Standard Deviation, Negative Control