Gp-120 Antigen

2020 ◽  
Author(s):  
Keyword(s):  
Gp 120

The presence or absence of gp 120/gp 160 bands on indeterminate Western blota

AIDS ◽  
1993 ◽  
Vol 7 (3) ◽  
pp. 437 ◽  
Author(s):  
R. King ◽  
S. Frey ◽  
R. Beisha ◽  
P. Van de Perre ◽  
E. Karita ◽  
...  
Keyword(s):  
Gp 120

scholarly journals In Vitro and In Silico Antioxidant, Anti-Diabetic, Anti-HIV and Anti-Alzheimer Activity of Endophytic Fungi, Cladosporium uredinicola Phytochemicals

2019 ◽  
Vol 13 ◽  
pp. 13-34
Author(s):  
Melappa Govindappa ◽  
V. Thanuja ◽  
S. Tejashree ◽  
C.A. Soukhya ◽  
Suresh Barge ◽  
...  
Keyword(s):  
Qualitative Method ◽  
Cholinesterase Activity ◽  
Methanol Extract ◽  
High Binding Energy ◽  
Acetyl Cholinesterase ◽  
Gp 120 ◽  
Anti Hiv ◽  
Hiv 1

The present work was aimed to identify phytochemicals in C. uredinicola methanol extract from qualitative, TLC and GC-MS method and evaluated for antioxidant, anti-HIV, anti-diabetes, anti-cholinesterase activity in vitro and in silico. The C. uredinicola extract showed flavonoids, tannins, alkaloids, glycosides, phenols, terpenoids, and coumarins presence in qualitative method. From GC-MS analysis, identified seven different phytochemicals and out of seven, four (coumarin, coumarilic acid, hymecromone, alloisoimperatorin) are coumarins. The C. uredinicola extract have shown significant antioxidant activity in DPPH (73) and FRAP (1359) method. The HIV-1 RT (83.81+2.14), gp 120 (80.24+2.31), integrase (79.43+3.14) and protease (77.63+2.14), DPPIV, β-glucosidase and acetyl cholinesterase activity was significantly reduced by the extract. The 2-diphenylmethyleneamino methyl ester had shown significant interaction with oxidant and HIV-1 proteins whereas alloisoimperatorin have interacted with diabetes and cholinesterase proteins followed by hymecromone with high binding energy. These three phytochemicals are non-carcinogens, non-toxic, readily degradable and have drug likeliness properties. The C. uredinicola phytochemicals are responsible for management of diabetes, HIV-1 and Alzheimer. Further in vivo work is needed to justify our research.

scholarly journals Posttransfusion purpura associated with an autoantibody directed against a previously undefined platelet antigen

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1458-1463
Author(s):  
RB Stricker ◽  
BH Lewis ◽  
L Corash ◽  
MA Shuman
Keyword(s):  
Acute Phase ◽  
Platelet Destruction ◽  
Autoantibody Production ◽  
Antiplatelet Antibodies ◽  
Platelet Protein ◽  
Gp 120 ◽  
Platelet Antigen ◽  
Immunoblot Technique ◽  
Posttransfusion Purpura ◽  
Acute Phase Serum

Although alloantibody against the PLA1 platelet antigen is usually found in patients with posttransfusion purpura (PTP), the mechanism of destruction of the patient's own PLA1-negative platelets is unexplained. We used a sensitive immunoblot technique to detect antiplatelet antibodies in a patient with classic PTP. The patient's acute-phase serum contained antibodies against three proteins present in control (PLA1-positive) platelets: an antibody that bound to a previously unrecognized platelet protein of mol wt 120,000 [glycoprotein (GP) 120], antibodies that bound to PLA1 (mol wt 90,000), and an epitope of GP IIb (mol wt 140,000). The antibodies against PLA1 and GP IIb did not react with the patient's own PLA1-negative platelets, control PLA1-negative platelets, or thrombasthenic platelets. In contrast, the antibody against GP 120 recognized this protein in all three platelet preparations, but not in Bernard-Soulier or Leka (Baka)-negative platelets. Antibody against GP 120 was not detected in the patient's recovery serum, although the antibodies against PLA1 and GP IIb persisted. F(ab)2 prepared from the patient's acute-phase serum also bound to GP 120. These results suggest that in PTP, transient autoantibody production may be responsible for autologous (PLA1-negative) platelet destruction. In addition, alloantibodies against more than one platelet alloantigen may be found in this disease. The nature of the GP 120 autoantigen and the GP IIb- related alloantigen defined by our patient's serum remains to be determined.

Demonstration of HIV-encoded Proteins in Cultured and in Uncultured CD 4 Positive Mononuclear Cells from Hemophilia Patients Employing Monoclonal Antibodies against p 15, p 24, GP 41, GP 120, and Reverse Transcriptase

1987 ◽  
Author(s):  
P Wernet ◽  
E M Scheider ◽  
P Sarin ◽  
P Chandra ◽  
H H Brackmann ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Reverse Transcriptase ◽  
Antigen Processing ◽  
Mononuclear Cells ◽  
Interleukin 2 ◽  
In Vitro Cultivation ◽  
Success Rates ◽  
Culture Techniques ◽  
Gp 120

In the light of the large percentage of hemophilia patients with antibodies to HIV the identification of a specific virus infection in comparison to HIV antibody negative hemophilia patients has reached crucial importance. The low success rates of direct virus culture techniques together with the as yet low AIDS-di-sease rate observed in these patients separate these patients from the other main risk groups. Within this context, we studied the expression of CD3, CD4, CD8, and HLA class II antigens on fixed cells after PHA stimulation and Interleukin 2 propagation as well as on untreated blood mononuclear cells from healthy individuals and from hemophilia patients by fluorescence activated flow cytometry. Monoclonal antibodies thought to be specific for p 15, p 24, GP 41, GP 120, and for reverse transcriptase revealed a certain number of positive cells on all defined subpopulations analysed. From cell specimen of HIV antibody positive hemophilia patients cells with specific HIV antigens could be enriched by in vitro cultivation. Importantly the expression of virus-encoded antigens preceedes a cytopathic effect for several daVs. Current analyses aim at the prognostic relevance of low amounts of such viral HIV proteins selectively detectable by moAbs.directed to either p 24, GP 41, GP 120, and RT. The reliability, high sensitivity and monoclonal antibody dependent specificity of this newly developed method for the demonstration of HIV specific proteins make it applicable also for longitudinal surveys of hemophilia patients to assess a potential state of viremia or virus antigen processing in their mononuclear cells.

scholarly journals Posttransfusion purpura associated with an autoantibody directed against a previously undefined platelet antigen

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1458-1463 ◽  
Author(s):  
RB Stricker ◽  
BH Lewis ◽  
L Corash ◽  
MA Shuman
Keyword(s):  
Acute Phase ◽  
Platelet Destruction ◽  
Autoantibody Production ◽  
Antiplatelet Antibodies ◽  
Platelet Protein ◽  
Gp 120 ◽  
Platelet Antigen ◽  
Immunoblot Technique ◽  
Posttransfusion Purpura ◽  
Acute Phase Serum

Abstract Although alloantibody against the PLA1 platelet antigen is usually found in patients with posttransfusion purpura (PTP), the mechanism of destruction of the patient's own PLA1-negative platelets is unexplained. We used a sensitive immunoblot technique to detect antiplatelet antibodies in a patient with classic PTP. The patient's acute-phase serum contained antibodies against three proteins present in control (PLA1-positive) platelets: an antibody that bound to a previously unrecognized platelet protein of mol wt 120,000 [glycoprotein (GP) 120], antibodies that bound to PLA1 (mol wt 90,000), and an epitope of GP IIb (mol wt 140,000). The antibodies against PLA1 and GP IIb did not react with the patient's own PLA1-negative platelets, control PLA1-negative platelets, or thrombasthenic platelets. In contrast, the antibody against GP 120 recognized this protein in all three platelet preparations, but not in Bernard-Soulier or Leka (Baka)-negative platelets. Antibody against GP 120 was not detected in the patient's recovery serum, although the antibodies against PLA1 and GP IIb persisted. F(ab)2 prepared from the patient's acute-phase serum also bound to GP 120. These results suggest that in PTP, transient autoantibody production may be responsible for autologous (PLA1-negative) platelet destruction. In addition, alloantibodies against more than one platelet alloantigen may be found in this disease. The nature of the GP 120 autoantigen and the GP IIb- related alloantigen defined by our patient's serum remains to be determined.

Two-site enzyme immunoassay of CD4 and CD8 molecules on the surface of T lymphocytes from healthy subjects and HIV-1-infected patients

1994 ◽  
Vol 40 (1) ◽  
pp. 30-37 ◽  
Author(s):  
D Carriere ◽  
C Fontaine ◽  
A M Berthier ◽  
A M Rouquette ◽  
P Carayon ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
T Lymphocytes ◽  
Enzyme Immunoassay ◽  
Cd8 T Cells ◽  
Envelope Glycoprotein ◽  
Healthy Subjects ◽  
Gp 120 ◽  
Highly Sensitive ◽  
One Step ◽  
Hiv 1

Abstract A highly sensitive two-site enzyme immunoassay (Capcellia) was developed to determine the concentration of CD4 and CD8 molecules expressed on the surface of human T lymphocytes. This assay, performed in one step (20 min), involves the specific immunocapture of T lymphocytes and reaction of the CD4 or CD8 molecules with an enzyme-labeled monoclonal antibody (mAb). The results were expressed as molar concentrations of the T-cell markers on the basis of results obtained with calibrated CD4 and CD8 standards. The assay was sensitive enough to detect 0.4 pmol/L CD4 or 0.8 pmol/L CD8, which corresponded to approximately 20 x 10(6) CD4+ or CD8+ T cells per liter of blood. Mean concentrations in healthy adults were 17.2 pmol/L for CD4 and 22.1 pmol/L for CD8. The CD4 concentration was < 8 pmol/L in 50% of HIV-1-infected patients and in 95% of AIDS patients. Given the epitopic specificity of the mAb to CD4 we used, these values correspond to the concentration of CD4 molecules free of envelope glycoprotein (gp)120.

Tin Protoporphyrin IX Used in Control of Heme Metabolism in Humans Effectively Inhibits HIV-1 Infection

1994 ◽  
Vol 5 (5) ◽  
pp. 322-330 ◽  
Author(s):  
A. R. Neurath ◽  
N. Strick ◽  
K. Lin ◽  
A. K. Debnath ◽  
S. Jiang
Keyword(s):  
Protoporphyrin Ix ◽  
V3 Loop ◽  
Gp 120 ◽  
Loop Sequence ◽  
Immunodeficiency Virus ◽  
Cd4 Binding Site ◽  
Glycoprotein Gp120 ◽  
Tin Protoporphyrin ◽  
Hiv 1

Recent observations indicated that several porphyrins bound to the V3 loop of the envelope glycoprotein gp120 of the human immunodeficiency virus type 1 (HIV-1) and inhibited infection of cells by HIV-1. The tin derivative of protoporphyrin IX (Sn-PTP-IX) has already been used clinically in humans to suppress hyperbilirubinemia. It was therefore of interest to determine whether Sn-PTP-IX has anti-HIV-1 activity. It is demonstrated here that Sn-PTP-IX effectively inhibited infection by several HIV-1 isolates (HIB, MN, RF, SF-2 and two isolates resistant to azidothymidine). This was surprising, since earlier studies indicated that incorporation of other metals into porphyrins markedly decreased their antiviral activity. Sn-PTP-IX blocked the binding to gp120 of anti-V3-loop-specific antibodies and of monoclonal antibodies specific for the CD4 binding site on gp120. The latter effect appeared to be allosteric and was not observed with a deletion mutant of gp 120 lacking the V3 loop sequence. This suggests that Sn-PTP-IX binds to the V3 loop and distorts the native conformation of the HIV-1 envelope, thereby preventing infection. These results merit the consideration of Sn-PTP-IX as a prophylactic and chemotherapeutic agent against HIV-1.

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