Immunization with a peptide mimicking lipoteichoic acid induces memory B cells in BALB/c mice.

Background: There is an urgent clinical need for developing novel immunoprophylaxis and immunotherapy strategies against Staphylococcus aureus (S. aureus). In our previous work, immunization with a tetra-branched multiple antigenic peptide, named MAP2-3 that mimics lipoteichoic acid, a cell wall component of S.

Immunization with a peptide mimicking Lipoteichoic acid protects mice against Staphylococcus aureus infection.

Lipoteichoic acid (LTA), a major component of the cell wall of Staphylococcus aureus (S. aureus), is not generally considered as an ideal vaccine candidate since it is a thymus-independent antigen. In this study, we screened a 12-mer phage peptide library and identified a series of peptide sequences that can mimic the epitope of LTA.

A Multiple Antigenic Peptide Mimicking Peptidoglycan Induced T Cell Responses to Protect Mice from Systemic Infection with Staphylococcus aureus.

Due to the enormous capacity of Staphylococcus aureus to acquire antibiotic resistance, it becomes imperative to develop vaccines for decreasing the risk of its life-threatening infections. Peptidoglycan (PGN) is a conserved and major component of S. aureus cell wall.

[A Paralytic shellfish poisoning GTX2,3 mimic peptide isolated from phage display: characterization and potential applications].

Aim: To screen peptide mimics of PSP (Paralytic shellfish poisoning) GTX2,3 from a random 12-mer phage display peptide library and to identify and characterize the specificity and accuracy of the peptide mimotope of GTX2,3.

Methods: The monoclonal antibody against GTX2,3 (mAb E(9);F(10);) was used as a target to screen the 12-mer phage display peptide library and the specificity of phage clones were identified by sandwich ELISA and blocking assay. The peptide sequences of positive phage clones were determined and analyzed by DNA sequencing.

Production and characterization of a cross-reactive monoclonal antibody to lipopolysaccharide.

Lipopolysaccharide (LPS) is located on the cell wall of gram-negative bacteria and plays an important role in the pathogenesis of sepsis, which continues to be a leading cause of death in the intensive care units. There are many strains and serotypes of gram-negative bacteria and each individual has a unique kind of LPS. In addition, LPS belongs to thymus-independent (TI) antigen, making it difficult to produce high-affinity, cross-reactive monoclonal antibodies (MAb) against LPS.

Advanced oxidation protein products induce mesangial cell perturbation through PKC-dependent activation of NADPH oxidase.

Mesangial deposition of extracellular matrix (ECM) is a hallmark of several glomerular diseases including diabetic nephropathy. Accumulation of advanced oxidation protein products (AOPPs) has been found in diabetes and chronic kidney disease and linked to mesangial ECM deposition and progressive glomerulosclerosis in these disorders. Although emerging evidence implicates AOPPs as the renal pathogenic factors, the underlying mechanisms have not been investigated.

[Computer-aided molecular modeling and activity estimation for ligand screening with specific phage clone as the target].

To investigate the interaction between tumor necrosis factor alpha (TNF alpha) mimotopes and TNF alpha-binding peptides screened from random phage display peptide library with TNF alpha mimotopes displayed on phage clone as the target, the computational docking program AutoDock (with confirmation calculations using Discover) was used to predict and analyze the binding modes of LLT-18 (TNF alpha binding peptide, sequence EHMALTYPFRPP) with TNF alpha, after which LCS-7 (TNF alpha mimic phage clone, displayed positive sequence c-RRPAQSG-c) was docked to LLT-18 manually. The binding between LLT-18 and TNF alpha or LCS-7 was stabilized predominantly through electrostatic interaction and H-bond formation. The Arg residues in TNF alpha or LCS-7 were important for their interaction with LLT-18.

[Screening of short peptides binding to cell surface interleukin-2 receptor alpha chain].

Objective: To screen and characterize the short peptides which bind specifically to interleukin-2 (IL-2) receptor alpha chain (IL-2Ralpha) for acquisition of small antagonists for blocking the binding of IL-2 with IL-2Ralpha.

Methods: 12-mer phage displayed peptide library was screened with the target cells of MT-2 cells which expressed IL-2Ralpha at high levels. The binding phage clones were eluted by anti-IL-2Ralpha monoclonal antibody.

[Screening of TNF-alpha mimotopes from c7c phage display peptide library].

Aim: To acquire oligo-peptides mimicking TNF-alpha epitopes.

Methods: The TNF-alpha mimotopes were screened from c7c phage display peptide library by using neutralizing mAb J1D9 against TNF-alpha, and positive clones were identified by sandwich ELISA.

Results: 9 out of 20 phage clones were identified as positive clones which can bind to mAb J1D9.

[Screening and identification of human telomerase reverse transcriptase epitopes from random phage display peptide library].

Objective: To identify and characterize the epitopes of human telomerase reverse transcriptase (hTERT).

Methods: A random phage displayed dodecapeptide library was screened with anti-hTERT antibody. The selected phage clones were identified by sandwich enzyme-linked immunosorbent assay, anti-hTERT antibody blocking assay and competitive inhibition assay.

[Screening of mimotope of Salmonella typhimurium lipopolysaccharide from phage-displayed peptide].

Objective: To identify and characterize the mimotope of lipopolysaccharide (LPS) from cyclic 7-mer phage peptide library.

Methods: Cyclic 7-mer phage-displayed peptide library was screened using monoclonal antibody 2F4 (mAb 2F4) against Salmonella typhimurium LPS as the target, and the selected clones were tested by sandwich enzyme-linked immunosorbent assay (ELISA) and specific antigen inhibition ELISA.

Results: After 3 round of screening, 34 of the 38 selected clones were identified as positive for binding to mAb 2F4.

[Screening of short peptides that bind specifically to osteosarcoma cells by phage-displayed peptide library].

Objective: To obtain short peptides which bind specifically to osteosarcoma cells os-732 by means of screening from 12 peptide libraries.

Methods: Osteosarcoma cells os-732 were used as the target cells and osteoblasts as the absorber cells for subtraction biopanning from a 12-mer peptide phage-display library. After 3 rounds of screening, the positive phage clones were identified by cell enzyme-linked immunosorbent assay (ELISA) and immunohistochemistry, and the amino acid sequences were deduced by DNA sequencing.