Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells.

Leonard, C K; Spellman, Michael W.; Riddle, Lavon; Harris, Reed J.; Thomas, Jordan; Gregory, Tim

doi:10.1016/s0021-9258(18)86956-3

Cited by 910 publications

(108 citation statements)

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“…In more detail, HIV enters the cells thanks to the envelope protein gp120 that engages the CD4 + -like receptor and the CCR5- or CXCR4-like coreceptor. After this interaction, the gp120 and gp41 peptides (glycosylated trimeric assemblies interacting with lectins) fuse inside the membrane [ 28 , 29 ] ( Figure 1 ).…”

Section: Microalgae Antiviral Compoundsmentioning

confidence: 99%

“…Chlorella pyrenoidosa produced an acid polysaccharide with some effects in mice against vesicular stomatitis virus (VSV) [ 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 ,…”

Section: Microalgae Antiviral Compoundsmentioning

confidence: 99%

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Evaluation of Microalgae Antiviral Activity and Their Bioactive Compounds

et al. 2021

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During the last year, science has been focusing on the research of antivirally active compounds overall after the SARS-CoV-2 pandemic, which caused a great amount of deaths and the downfall of the economy in 2020. Photosynthetic organisms such as microalgae are known to be a reservoir of bioactive secondary metabolites; this feature, coupled with the possibility of achieving very high biomass levels without excessive energetic expenses, make microalgae worthy of attention in the search for new molecules with antiviral effects. In this work, the antiviral effects of microalgae against some common human or animal viruses were considered, focusing our attention on some possible effects against SARS-CoV-2. We summed up the data from the literature on microalgae antiviral compounds, from the most common ones, such as lectins, polysaccharides and photosynthetic pigments, to the less known ones, such as unidentified proteins. We have discussed the effects of a microalgae-based genetic engineering approach against some viral diseases. We have illustrated the potential antiviral benefits of a diet enriched in microalgae.

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Section: Microalgae Antiviral Compoundsmentioning

confidence: 99%

Section: Microalgae Antiviral Compoundsmentioning

confidence: 99%

Evaluation of Microalgae Antiviral Activity and Their Bioactive Compounds

et al. 2021

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“…3 Gp120 has 24 asparagine (N) linked carbohydrate chains (referred to as N-glycans) which "camouflage" (mask) a large proportion of the antigenic peptides and are referred to as the "glycan-shield". [3][4][5][6] Synthesis of glycans due to mutations that form more glycosylation sites (i.e., the sequon N-X-S/T) contributes to additional masking of gp120 antigens and thus, to evasion from the anti-HIV neutralizing antibodies. 3 The S-protein of SARS-CoV-2 has 22 N-glycans.…”

Section: The Variants Conundrum In Gene-based Vs Whole-virus Vaccinesmentioning

confidence: 99%

“…O-glycans (linked to serine or threonine) on the viral glycoproteins also carry SA. [4][5][6][7][8][9] An example of SA on N-glycans of a glycoprotein is illustrated as the left glycan in Figure 1. The same glycans are present on APC and on other cells in the body.…”

Section: Immunogenicity Of Enveloped Whole-virus Vaccinesmentioning

confidence: 99%

“…10 Antigen-masking by the glycan-shield-It is estimated that the glycan-shields on viruses such as HIV and SARS-CoV-2 cover ~65% of the surface of the gp120 and S-protein, respectively. [3][4][5][6][7][8] In addition, there are Oglycosylated glycan on viral glycoproteins which together with the N-glycans mask many of the antigenic peptides from recognition by B cell receptors and by the corresponding antibodies. The combination of negative charge repulsion by sialic acids and masking of antigenic peptides by the glycan-shield results in suboptimal efficacy of some inactivated virus vaccines for stimulation of the immune system in vaccinated individuals.…”

Section: Immunogenicity Of Enveloped Whole-virus Vaccinesmentioning

confidence: 99%

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Increasing Efficacy of Enveloped Whole-Virus Vaccines by In situ Immune-Complexing with the Natural Anti-Gal Antibody

Galili

2021

MRAJ

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The appearance of variants of mutated virus in course of the Covid-19 pandemic raises concerns regarding the risk of possible formation of variants that can evade the protective immune response elicited by the single antigen S-protein gene-based vaccines. This risk may be avoided by inclusion of several antigens in vaccines, so that a variant that evades the immune response to the S-protein of SARS-CoV-2 virus will be destroyed by the protective immune response against other viral antigens. A simple way for preparing multi-antigenic enveloped-virus vaccines is using the inactivated whole-virus as vaccine. However, immunogenicity of such vaccines may be suboptimal because of poor uptake of the vaccine by antigen-presenting-cells (APC) due to electrostatic repulsion by the negative charges of sialic-acid on both the glycan-shield of the vaccinating virus and on the carbohydrate-chains (glycans) of APC. In addition, glycan-shield can mask many antigenic peptides. These effects of the glycan-shield can be reduced and immunogenicity of the vaccinating virus markedly increased by glycoengineering viral glycans for replacing sialic-acid units on glycans with a-gal epitopes (Gala1-3Galb1-4GlcNAc-R). Vaccination of humans with inactivated whole-virus presenting a-gal epitopes (virusa-gal) results in formation of immune-complexes with the abundant natural anti-Gal antibody that binds to viral a-gal epitopes at the vaccination site. These immune-complexes are targeted to APC for rigorous uptake due to binding of the Fc portion of immunocomplexed anti-Gal to Fcg receptors on APC. The APC further transport the large amounts of internalized vaccinating virus to regional lymph nodes, process and present the virus antigenic peptides for the activation of many clones of virus specific helper and cytotoxic T-cells. This elicits a protective cellular and humoral immune response against multiple viral antigens and an effective immunological memory. The immune response to virusa-gal vaccine was studied in mice producing anti-Gal and immunized with inactivated influenza-virusa-gal. These mice demonstrated 100-fold increase in titer of the antibodies produced, a marked increase in T-cell response, and a near complete protection against challenge with a lethal dose of live influenza-virus, in comparison to a similar vaccine lacking a-gal epitopes. This glycoengineering can be achieved in vitro by enzymatic reaction with neuraminidase removing sialic-acid and with recombinant a1,3galactosyltransferase (a1,3GT) synthesizing a-gal epitopes, by engineering host-cells to contain several copies of the a1,3GT gene (GGTA1), or by transduction of this gene in a replication-defective adenovirus vector into host-cells. Theoretically, these methods for increased immunogenicity may be applicable to all enveloped viruses with N-glycans on their envelope.

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Prediction of the secondary structure of HIV-1 gp120

et al. 1996

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The secondary structure of HIV‐1 gp120 was predicted using multiple alignment and a combination of two independent methods based on neural network and nearest‐neighbor algorithms. The methods agreed on the secondary structure for 80% of the residues in BH10 gp120. Six helices were predicted in HIV strain BH10 gp120, as well as in 27 other HIV‐1 strains examined. Two helical segments were predicted in regions displaying profound sequence variation, one in a region suggested to be critical for CD4 binding. The predicted content of helix, β‐strand, and coil was consistent with estimates from Fourier transform infrared spectroscopy. The predicted secondary structure of gp120 compared well with data from NMR analysis of synthetic peptides from the V3 loop and the C4 region. As a first step towards modeling the tertiary structure of gp120, the predicted secondary structure may guide the design of future HIV sub‐unit vaccine candidates. © 1996 Wiley‐Liss, Inc.

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Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells.

Cited by 910 publications

References 45 publications

Evaluation of Microalgae Antiviral Activity and Their Bioactive Compounds

Evaluation of Microalgae Antiviral Activity and Their Bioactive Compounds

Increasing Efficacy of Enveloped Whole-Virus Vaccines by In situ Immune-Complexing with the Natural Anti-Gal Antibody

Prediction of the secondary structure of HIV-1 gp120

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