Outer membrane protein OmpW of Escherichia coli is required for resistance to phagocytosis.

Eight-stranded β-barrel outer membrane proteins can confer bacterial virulence via resistance to host innate defenses. This resistance function of OmpW, which was recently identified as an eight-stranded β-barrel protein, was investigated in this study. Our results demonstrated that upregulation of OmpW correlated with increased bacterial survival during phagocytosis.

Alterations of protein complexes and pathways in genetic information flow and response to stimulus contribute to Escherichia coli resistance to balofloxacin.

Protein-protein interactions are important biological processes and essential for a global understanding of cell functions. To date, little is known about the protein interactions and roles of the protein interacting networks and protein complexes in bacterial resistance to antibiotics. In the present study, we investigated protein complexes in Escherichia coli exposed to an antibiotic balofloxacin (BLFX).

Comparative proteomic analysis of colon cancer cell HCT-15 in response to all-trans retinoic acid treatment.

Colon cancer is one of the most common malignances. In vitro and in vivo study show that retinoic acids inhibit a wide variety of cancer cells but the molecular mechanism of their anti-tumor effects are not yet fully understood. Alltrans retinoic acid (ATRA), an isomer of retinoic acid, can inhibit the proliferation of HCT-15 human colon cancer cell line.

Complexome of Escherichia coli cytosolic proteins under normal native conditions.

The interactions between proteins are important for the majority of biological functions and the interacting proteins are usually assembled into a complex. Knowing a set of protein complexes of a cell (complexome) is, therefore, essential for a better understanding and global view of cell functions. To visualize and identify the protein complexome of E.

Isolation and characterization of Hainantoxin-II, a new neurotoxic peptide from the Chinese bird spider (Haplopelma hainanum).

Hainantoxin-II (HnTx-II), a novel neurotoxin, was isolated from the venom of the Chinese bird spider (Haplopelma hainanum) by cation exchange chromatography and reverse-phase HPLC. The toxin was a single chain polypeptide with calculated molecular weight of 4 253.135 obtained by mass spectrometry.

Complexome of Escherichia coli envelope proteins under normal physiological conditions.

The interactions between proteins are important for very numerous, if not all, biological functions, and the interacted proteins might form part of a protein complex. To understand the protein complexes of a cell, complexome, is essential for a better understanding of cell functions. In the present study, we have performed a systematic fractionation and analysis of Escherichia coli K-12 membrane proteins under proximately normal physiological conditions using two-dimensional native/SDS-PAGE (N-PAGE)-based proteomics.

Dodecamer is required for agglutination of Litopenaeus vannamei hemocyanin with bacterial cells and red blood cells.

Hemocyanins are multi-functional proteins, although they are well known to be respiratory proteins of invertebrate to date. In the present study, the agglutination ability of two oligomers of hemocyanin, hexamer and dodecamer, with pathogenic bacteria and red blood cells (RBCs) is investigated in pacific white shrimp, Litopenaeus vannamei. Hexameric hemocyanin exhibits an extremely high stability even in the absence of Ca(2+) and in alkaline pH.