Retraction for Khattar et al., “Newcastle Disease Virus Expressing Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Induces Strong Mucosal and Serum Antibody Responses in Guinea Pigs”

ABSTRACT One attractive strategy for the development of a human immunodeficiency virus (HIV) vaccine is the use of viral vectors with a proven safety profile and an absence of preexisting immunity in humans, such as Newcastle disease virus (NDV). Several NDV vaccine vectors have been generated, and their immunogenicities have been investigated with different animal models. However, a systematic study to evaluate the optimal insertion site of the foreign antigens into NDV that results in enhanced immune responses specific to the antigen has not yet been conducted. In this article, we describe the ability of NDV expressing HIV Gag to generate a Gag-specific immune response in mice. We also have determined the optimal insertion site into the NDV genome by generating recombinant NDV-HIVGag viruses in which HIV gag was located at different transcriptional positions throughout the NDV viral genome. All recombinant viruses were viable, grew to similar titers in embryonated chicken eggs, and expressed Gag in a stable manner. Our in vivo experiments revealed that higher HIV Gag protein expression positively correlates with an enhanced CD8+ T-cell-mediated immune response and protective immunity against challenge with vaccinia virus expressing HIV Gag. We also inserted a codon-optimized version of HIV gag in the described best location, between the P and M genes. Virus expressing the codon-optimized version of HIV gag induced a higher expression of the protein and an enhanced immune response against HIV Gag in mice. These results indicate that strategies directed toward increasing antigen expression by NDV result in enhanced immunogenicity and vaccine efficacy.

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Characterization of the Outer Domain of the gp120 Glycoprotein from Human Immunodeficiency Virus Type 1

Journal of Virology ◽

10.1128/jvi.78.23.12975-12986.2004 ◽

2004 ◽

Vol 78 (23) ◽

pp. 12975-12986 ◽

Cited By ~ 51

Author(s):

Xinzhen Yang ◽

Vesko Tomov ◽

Svetla Kurteva ◽

Liping Wang ◽

Xinping Ren ◽

...

Keyword(s):

Human Immunodeficiency Virus ◽

Human Immunodeficiency Virus Type ◽

Virus Type ◽

Envelope Glycoprotein ◽

Antibody Responses ◽

Outer Domain ◽

Immunodeficiency Virus ◽

Gp120 Glycoprotein ◽

Hiv 1

ABSTRACT The core of the gp120 glycoprotein from human immunodeficiency virus type 1 (HIV-1) is comprised of three major structural domains: the outer domain, the inner domain, and the bridging sheet. The outer domain is exposed on the HIV-1 envelope glycoprotein trimer and contains binding surfaces for neutralizing antibodies such as 2G12, immunoglobulin G1b12, and anti-V3 antibodies. We expressed the outer domain of HIV-1YU2 gp120 as an independent protein, termed OD1. OD1 efficiently bound 2G12 and a large number of anti-V3 antibodies, indicating its structural integrity. Immunochemical studies with OD1 indicated that antibody responses against the outer domain of the HIV-1 gp120 envelope glycoprotein are rare in HIV-1-infected human sera that potently neutralize the virus. Surprisingly, such outer-domain-directed antibody responses are commonly elicited by immunization with recombinant monomeric gp120. Immunization with soluble, stabilized HIV-1 envelope glycoprotein trimers elicited antibody responses that more closely resembled those in the sera of HIV-1-infected individuals. These results underscore the qualitatively different humoral immune responses elicited during natural infection and after gp120 vaccination and help to explain the failure of gp120 as an effective vaccine.

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Immunization of cattle with recombinant Newcastle disease virus expressing bovine herpesvirus-1 (BHV-1) glycoprotein D induces mucosal and serum antibody responses and provides partial protection against BHV-1

Vaccine ◽

10.1016/j.vaccine.2010.02.051 ◽

2010 ◽

Vol 28 (18) ◽

pp. 3159-3170 ◽

Cited By ~ 43

Author(s):

Sunil K. Khattar ◽

Peter L. Collins ◽

Siba K. Samal

Keyword(s):

Newcastle Disease Virus ◽

Disease Virus ◽

Newcastle Disease ◽

Serum Antibody ◽

Bovine Herpesvirus ◽

Antibody Responses ◽

Bovine Herpesvirus 1 ◽

Partial Protection ◽

Herpesvirus 1 ◽

Recombinant Newcastle Disease Virus

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Biochemical and Immunogenic Characterization of Soluble Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers Expressed by Semliki Forest Virus

Journal of Virology ◽

10.1128/jvi.79.17.10902-10914.2005 ◽

2005 ◽

Vol 79 (17) ◽

pp. 10902-10914 ◽

Cited By ~ 31

Author(s):

Mattias N. E. Forsell ◽

Yuxing Li ◽

Maria Sundbäck ◽

Krisha Svehla ◽

Peter Liljeström ◽

...

Keyword(s):

Human Immunodeficiency Virus ◽

Immune Responses ◽

Envelope Glycoprotein ◽

Neutralizing Antibodies ◽

Semliki Forest Virus ◽

Neutralizing Antibody ◽

Antibody Responses ◽

Immunodeficiency Virus ◽

Hiv 1

ABSTRACT The current lack of envelope glycoprotein immunogens that elicit broadly neutralizing antibody responses remains a major challenge for human immunodeficiency virus type 1 (HIV-1) vaccine development. However, the recent design and construction of stable soluble gp140 trimers have shown that some neutralization breadth can be achieved by using immunogens that better mimic the functional viral spike complex. The use of genetic delivery systems to drive the in vivo expression of such immunogens for the stimulation of neutralizing antibodies against HIV-1 may offer advantages by maintaining the quaternary structure of the trimeric envelope glycoproteins. Here, we describe the biochemical and immunogenic properties of soluble HIV-1 envelope glycoprotein trimers expressed by recombinant Semliki Forest virus (rSFV). The results presented here demonstrate that rSFV supports the expression of stable soluble gp140 trimers that retain recognition by conformationally sensitive antibodies. Further, we show that rSFV particle immunizations efficiently primed immune responses as measured after a single boost with purified trimeric gp140 protein, resulting in a Th1-biased antibody response. This differed from the Th2-biased antibody response obtained after repeated immunizations with purified gp140 protein trimers. Despite this difference, both regimens stimulated neutralizing antibody responses of similar potency. This suggests that rSFV may be a useful component of a viral vector prime-protein boost regimen aimed at stimulating both cell-mediated immune responses and neutralizing antibodies against HIV-1.

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Comparison of Neutralizing and Hemagglutination-Inhibiting Antibody Responses to Influenza A Virus Vaccination of Human Immunodeficiency Virus-Infected Individuals

Clinical and Diagnostic Laboratory Immunology ◽

10.1128/cdli.5.1.114-117.1998 ◽

1998 ◽

Vol 5 (1) ◽

pp. 114-117 ◽

Cited By ~ 23

Author(s):

C. A. Benne ◽

F. P. Kroon ◽

M. Harmsen ◽

L. Tavares ◽

C. A. Kraaijeveld ◽

...

Keyword(s):

Human Immunodeficiency Virus ◽

Influenza Virus ◽

Influenza A ◽

Serum Antibody ◽

Influenza Virus Infection ◽

Antibody Responses ◽

Immunodeficiency Virus ◽

Antibody Titers ◽

Hiv Type 1

ABSTRACT A neutralization enzyme immunoassay (N-EIA) was used to determine the neutralizing serum antibody titers to influenza A/Taiwan/1/86 (H1N1) and Beijing/353/89 (H3N2) viruses after vaccination of 51 human immunodeficiency virus (HIV) type 1-infected individuals and 10 healthy noninfected controls against influenza virus infection. Overall, the N-EIA titers correlated well with the hemagglutination-inhibition (HAI) titers that were observed in the same samples in a previous study (F. P. Kroon, J. T. van Dissel, J. C. de Jong, and R. van Furth, AIDS 8:469–476,1994). The N-EIA appeared to be more sensitive than the HAI test. Significantly more fourfold or higher rises in N-EIA titer and higher mean N-EIA titers occurred in HIV-infected individuals with ≥200 CD4+ cells per μl than in those with <200 CD4+ cells per μl.

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