scholarly journals Ahmpatinin iBu, a new HIV-1 protease inhibitor, from Streptomyces sp. CPCC 202950

RSC Advances ◽  
2018 ◽  
Vol 8 (10) ◽  
pp. 5138-5144 ◽  
Author(s):  
Ming-Hua Chen ◽  
Shan-Shan Chang ◽  
Biao Dong ◽  
Li-Yan Yu ◽  
Ye-Xiang Wu ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Inhibitory Activity ◽  
Streptomyces Sp ◽  
Hiv 1

Ahmpatinin iBu and statinin iBu, two new linear peptides, were isolated from Streptomyces sp. CPCC 202950. Ahmpatinin iBu exhibited significant inhibitory activity against HIV-1 protease with an IC50 value of 1.79 nM.

Time-Resolved Fluorescence Anisotropy of HIV-1 Protease Inhibitor Complexes Correlates with Inhibitory Activity†

Biochemistry ◽  
1998 ◽  
Vol 37 (9) ◽  
pp. 2778-2786 ◽  
Author(s):  
A. J. Kungl ◽  
N. V. Visser ◽  
A. van Hoek ◽  
A. J. W. G. Visser ◽  
A. Billich ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Fluorescence Anisotropy ◽  
Inhibitory Activity ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Hiv 1

scholarly journals Inhibition of Human Immunodeficiency Virus Type 1 Infectivity by Secretory Leukocyte Protease Inhibitor Occurs Prior to Viral Reverse Transcription

Blood ◽  
1997 ◽  
Vol 90 (3) ◽  
pp. 1141-1149 ◽  
Author(s):  
Tessie B. McNeely ◽  
Diane C. Shugars ◽  
Mary Rosendahl ◽  
Christina Tucker ◽  
Stephen P. Eisenberg ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Protease Inhibitor ◽  
Viral Infection ◽  
Reverse Transcription ◽  
Inhibitory Activity ◽  
Virus Binding ◽  
Viral Dna ◽  
Immunodeficiency Virus ◽  
Anti Hiv ◽  
Hiv 1

Abstract Infection of monocytes with human immunodeficiency virus type 1Ba-L (HIV-1Ba-L ) is significantly inhibited by treatment with the serine protease inhibitor, secretory leukocyte protease inhibitor (SLPI). SLPI does not appear to act on virus directly, but rather the inhibitory activity is most likely due to interaction with the host cell. The current study was initiated to investigate how SLPI interacts with monocytes to inhibit infection. SLPI was found to bind to monocytes with high affinity to a single class of receptor sites (∼7,000 receptors per monocyte, KD = 3.6 nmol/L). The putative SLPI receptor was identified as a surface protein with a molecular weight of 55 ± 5 kD. A well-characterized function of SLPI is inhibition of neutrophil elastase and cathepsin G. However, two SLPI mutants (or muteins) that contain single amino acid substitutions and exhibit greatly reduced protease inhibitory activity still bound to monocytes and retained anti–HIV-1 activity. SLPI consists of two domains, of which the C-terminal domain contains the protease inhibiting region. However, when tested independently, neither domain had potent anti–HIV-1 activity. SLPI binding neither prevented virus binding to monocytes nor attenuated the infectivity of any virus progeny that escaped inhibition by SLPI. A polymerase chain reaction (PCR)-based assay for newly generated viral DNA demonstrated that SLPI blocks at or before viral DNA synthesis. Therefore, it most likely inhibits a step of viral infection that occurs after virus binding but before reverse transcription. Taken together, the unique antiviral activity of SLPI, which may be independent of its previously characterized antiprotease activity, appears to reside in disruption of the viral infection process soon after virus binding.

scholarly journals Inhibition of Human Immunodeficiency Virus Type 1 Infectivity by Secretory Leukocyte Protease Inhibitor Occurs Prior to Viral Reverse Transcription

Blood ◽  
1997 ◽  
Vol 90 (3) ◽  
pp. 1141-1149 ◽  
Author(s):  
Tessie B. McNeely ◽  
Diane C. Shugars ◽  
Mary Rosendahl ◽  
Christina Tucker ◽  
Stephen P. Eisenberg ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Protease Inhibitor ◽  
Viral Infection ◽  
Reverse Transcription ◽  
Inhibitory Activity ◽  
Virus Binding ◽  
Viral Dna ◽  
Immunodeficiency Virus ◽  
Anti Hiv ◽  
Hiv 1

Infection of monocytes with human immunodeficiency virus type 1Ba-L (HIV-1Ba-L ) is significantly inhibited by treatment with the serine protease inhibitor, secretory leukocyte protease inhibitor (SLPI). SLPI does not appear to act on virus directly, but rather the inhibitory activity is most likely due to interaction with the host cell. The current study was initiated to investigate how SLPI interacts with monocytes to inhibit infection. SLPI was found to bind to monocytes with high affinity to a single class of receptor sites (∼7,000 receptors per monocyte, KD = 3.6 nmol/L). The putative SLPI receptor was identified as a surface protein with a molecular weight of 55 ± 5 kD. A well-characterized function of SLPI is inhibition of neutrophil elastase and cathepsin G. However, two SLPI mutants (or muteins) that contain single amino acid substitutions and exhibit greatly reduced protease inhibitory activity still bound to monocytes and retained anti–HIV-1 activity. SLPI consists of two domains, of which the C-terminal domain contains the protease inhibiting region. However, when tested independently, neither domain had potent anti–HIV-1 activity. SLPI binding neither prevented virus binding to monocytes nor attenuated the infectivity of any virus progeny that escaped inhibition by SLPI. A polymerase chain reaction (PCR)-based assay for newly generated viral DNA demonstrated that SLPI blocks at or before viral DNA synthesis. Therefore, it most likely inhibits a step of viral infection that occurs after virus binding but before reverse transcription. Taken together, the unique antiviral activity of SLPI, which may be independent of its previously characterized antiprotease activity, appears to reside in disruption of the viral infection process soon after virus binding.

A Novel Ribonuclease with HIV-1 Reverse Transcriptase Inhibitory Activity from the Edible Mushroom Hygrophorus russula

2013 ◽  
Vol 170 (1) ◽  
pp. 219-230 ◽  
Author(s):  
Mengjuan Zhu ◽  
Lijing Xu ◽  
Xiao Chen ◽  
Zengqiang Ma ◽  
Hexiang Wang ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Inhibitory Activity ◽  
Edible Mushroom ◽  
Hiv 1

Synthesis and HIV-1 integrase inhibitory activity of dimeric and tetrameric analogs of indolicidin

2004 ◽  
Vol 14 (22) ◽  
pp. 5595-5598 ◽  
Author(s):  
Krzysztof Krajewski ◽  
Christophe Marchand ◽  
Ya-Qiu Long ◽  
Yves Pommier ◽  
Peter P. Roller
Keyword(s):  
Inhibitory Activity ◽  
Hiv 1
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