Evaluation of the effectiveness of ultrasound-guided transversus abdominis plane (TAP) block for chronic pain after lower abdominal surgery

Aim: This study aimed to evaluate the effectiveness of ultrasound-guided transversus abdominis plane (TAP) block in patients diagnosed with chronic pain after undergoing lower abdominal surgery. Methods: Patients who were admitted to the pain medicine clinic between January 1, 2016, and January 1, 2020, and underwent TAP block with the diagnosis of chronic pain after undergoing lower abdominal surgery were retrospectively analyzed. The visual analog scale (VAS) score was measured before the procedure and at the 1-month and 3-month follow-ups. Results: The proportion of patients with a reduction in VAS scores of >50% after TAP block application was 50% at the 1-month follow-up and 72.5% at the 3-month follow-up. The changes in the VAS score was found to be statistically significant (p < 0.05). Conclusion: Although ultrasound-guided TAP block seems to be an effective treatment method for chronic pain after lower abdominal surgery, further studies and clinical trials investigating different types of surgeries and including a larger number of patients are warranted

Human Cytomegalovirus Fcγ Binding Proteins gp34 and gp68 Antagonize Fcγ Receptors I, II and III

Human cytomegalovirus (HCMV) establishes lifelong infection with recurrent episodes of virus production and shedding despite the presence of adaptive immunological memory responses including HCMV immune immunoglobulin G (IgG). Very little is known how HCMV evades from humoral and cellular IgG-dependent immune responses, the latter being executed by cells expressing surface receptors for the Fc domain of IgG (FcγRs). Remarkably, HCMV expresses the RL11-encoded gp34 and UL119-118-encoded gp68 type I transmembrane glycoproteins which bind Fcγ with nanomolar affinity. Using a newly developed FcγR activation assay, we tested if the HCMV-encoded Fcγ binding proteins (HCMV FcγRs) interfere with individual host FcγRs. In absence of gp34 or/and gp68, HCMV elicited a much stronger activation of FcγRIIIA/CD16, FcγRIIA/CD32A and FcγRI/CD64 by polyclonal HCMV-immune IgG as compared to wildtype HCMV. gp34 and gp68 co-expression culminates in the late phase of HCMV replication coinciding with the emergence of surface HCMV antigens triggering FcγRIII/CD16 responses by polyclonal HCMV-immune IgG. The gp34- and gp68-dependent inhibition of HCMV immune IgG was fully reproduced when testing the activation of primary human NK cells. Their broad antagonistic function towards FcγRIIIA, FcγRIIA and FcγRI activation was also recapitulated in a gain-of-function approach based on humanized monoclonal antibodies (trastuzumab, rituximab) and isotypes of different IgG subclasses. Surface immune-precipitation showed that both HCMV-encoded Fcγ binding proteins have the capacity to bind trastuzumab antibody-HER2 antigen complexes demonstrating simultaneous linkage of immune IgG with antigen and the HCMV inhibitors on the plasma membrane. Our studies reveal a novel strategy by which viral FcγRs can compete for immune complexes against various Fc receptors on immune cells, dampening their activation and antiviral immunity.DFG grant He 2526/6-2.European Commission grants QLRT-2001-01112 and MRTN-CT-2005-019248.Helmholtz Association through VISTRIE VH-VI-242.UCR::Vicerrectoría de Docencia::Salud::Facultad de Microbiologí

Feasibility of Mammary Ductoscopy in Management of Pathologic Nipple Discharge

16th Annual Meeting of the American-Society-of-Breast-Surgeons -- APR 29-MAY 03, 2015 -- Orlando, FL[No Abstract Available]Amer Soc Breast Sur

Ectopic expression of HSV-1 gE, HCMV gp68 and HCMV gp34 inhibit IgG1 (trastuzumab) mediated activation of FcγRs.

<p>(<b>A</b>) SKOV-3 cells were infected for 24 h with 2 PFU/cell VACV wt and rVACV expressing gE or (<b>B</b>) rVACV expressing gp68 or gp34 before opsonized with trastuzumab at different concentrations for 30 min. After removing of unbound antibodies by repeated washing with D-MEM 10% (vol/vol) FCS, 1×10⁵ BW:FcγR-ζ transfectants per well were added and co-cultivated overnight. BW:FcγR-ζ activation was determined by measuring mIL-2 by ELISA. Three independent replicates were measured, means with standard deviations (error bars) are shown for 3 independent experiments. Significance of results (Student's t-test) are presented in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004131#ppat.1004131.s006" target="_blank">Table S1</a> as *: p<0.05 **: p<0.01 ***: p<0.001.</p

HCMV gp68 and gp34 inhibit FcγRIII activation by rituximab antibody isotypes.

<p>CD20 transfected 293T cells were infected for 16/cell of VACV wt or rVACV expressing gp68, gp34 or MULT-1 as a control. After opsonization with 1 µg/ml of each antibody isotype for 30 min. and removing of unbound antibody by washing, cells were co-cultivated with 1×10⁵ BW:FcγRIIIA-ζ reporter cells per well for 16 h before supernatants were collected and mIL-2 was determined by ELISA. Each value represents three replicates; means with standard deviations (error bars) are shown for 2 independent experiments. Significance of results (Student's t-test) are presented in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004131#ppat.1004131.s006" target="_blank">Table S1</a> as *: p<0.05 **: p<0.01 ***: p<0.001.</p

Soluble ectodomains of HCMV vFcγR interfere with antibody dependent NK cell degranulation.

<p>(<b>A</b>) Cytotect was coated to a plate in binding buffer (0.1 M Na₂HPO₄ pH 9.0) at a concentration of 0.5 mg/ml and incubated for 2.5 hours at 37°C. After blocking for 30 minutes and washing unbound antibodies, soluble proteins, rIL-2 pre-activated primary NK cells and α-CD107a-PECy5 antibody were added and incubated for 4 hours at 37°C. Duplicates were measured for CD107a surface expression after dead cell exclusion with DAPI staining in a FACS Canto II. Means are shown with standard deviations (error bars). Significance of results (Student's t-test) are presented in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004131#ppat.1004131.s006" target="_blank">Table S1</a> as *: p<0.05 **: p<0.01 ***: p<0.001. (<b>B</b>) To compare the amounts of soluble proteins used in (A), SDS-PAGE and anti-V5 immunobotting was performed.</p

HSV-1 gE, HCMV gp68 and HCMV gp34 interfere with host FcγR activation upon opsonization of cells with polyclonal immune IgG.

<p>(<b>A</b>) The HSV vFcγR gE inhibits FcγRIIIA and FcγRIIA activation but fails to inhibit FcγRI. Human MRC-5 fibroblasts were infected with 2 PFU/cell of HSV-1 strain F wt and ΔgE for 24 h. Cells were opsonized with Cytotect at different concentrations for 30 min. After removing of unbound antibodies with D-MEM 10% (vol/vol) FCS, 1×10⁵ BW:FcγR-ζ transfectants per well were added and co-cultivated overnight. BW:FcγR activation was determined by measuring mIL-2 by ELISA. Three independent replicates were measured; means with standard deviations (error bars) are shown for 4 independent experiments. (<b>B</b>) HCMV vFcγR gp68 interferes with FcγRIIIA, FcγRIIA and FcγRI activation. MRC-5 cells were infected with HCMV HB5 wt virus or HB5Δgp68 (2 PFU/cell) for 72 h. Fibroblasts were opsonized with Cytotect at different concentrations for 30 min. After removing of unbound antibodies by washing, 1×10⁵ BW:FcγR-ζ transfectants were added per well. Measurement of mIL-2 in supernatants after 16 h of co-cultivation of reporter cells with targets was performed by ELISA. Values are presented in the graphic as OD 450 nm. Three independent wells were measured; means with standard deviations (error bars) are shown for 4 independent experiments. Significance of results (Student's t-test) are presented in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004131#ppat.1004131.s006" target="_blank">Table S1</a> as *: p<0.05 **: p<0.01 ***: p<0.001. (<b>C</b>) HCMV vFcγR gp34 interferes with FcγRIIIA, FcγRIIA and FcγRI activation. As in (B) but MRC-5 cells were infected with HCMV HB5ΔIRL, HB5ΔIRLΔgp34 or HB5ΔIRLΔgp68/Δgp34 (2 PFU/cell) for 72 h. (<b>D</b>) gp34 and gp68 interfere with FcγR activation in AD169varL infected cells. As in (B) but MRC-5 cells were infected with AD169varL wt, AD169varLΔgp68, AD169varLΔgp34 or AD169varLΔgp68/Δgp34.</p

The HCMV vFcγRs gp68 and gp34 bind antigen-IgG complexes.

<p>(<b>A</b>) Schematic representation of the ‘antibody bipolar bridging’ model. (<b>B</b>) Lysates of SKOV-3 cells containing the heterocomplex of vFcγR-FLAG, antibody and antigen are immunoprecipitated using an anti-FLAG agarose. SKOV-3 cells expressing HER2 antigen on the surface were infected with rVACV expressing the vFcγRs before opsonized with the trastuzumab antibody (bipolar bridging-antibody) (T) or an isotype control IgG1 antibody, palivizumab (P). Lysates were prepared after incubation of infected cells with antibody. An anti-Flag agarose IP was performed and retrieved antigens were detected in western blot with anti-ErbB2-specific mAb recognizing human HER2, anti-human IgG, and anti-Flag (M2, Sigma-Aldrich) detecting the Flag-tagged vFcγRs. Equal expression of HER2 in cell lysates was verified by western blot analysis with an anti-ErbB2-specific rabbit mAb which detects human HER2 (bottom).</p