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Journal of Virology, November 2000, p. 10025-10033, Vol. 74, No. 21
Veterans Affairs Medical Center and New York
University School of Medicine, New York, New
York1; St. Louis University, St.
Louis, Missouri2; Chiron Corporation,
Emeryville, California3; and Aventis
Pasteur, Campus Merieux, Marcy L'Etoile, France4
Received 3 May 2000/Accepted 21 July 2000
A human immunodeficiency virus (HIV) vaccine that will be useful in
diverse geographic regions will need to induce a broad immune response
characterized by cross-clade immunity. To test whether a clade B-based
HIV candidate vaccine could induce interclade humoral responses,
including neutralizing activity against primary HIV-1 isolates, sera
were tested from recipients of a vaccine consisting of recombinant
canarypox virus vCP205 and recombinant gp120SF2. Serum
antibodies exhibited strong immunochemical cross-reactivity with V3
peptides from clades B, C, and F, with weaker activity for several V3
peptides from clades A, D, G, and H; essentially no reactivity could be
demonstrated with V3 peptides from clades E and O. Extensive
cross-clade reactivity was also documented by enzyme-linked
immunosorbent assay with all nine recombinant HIV envelope
glycoproteins tested from clades B, D, and E. In addition, vaccinees'
sera displayed significant neutralizing activity against 5 of 14 primary isolates tested, including one X4 virus and two dualtropic
viruses (from clade B) and two R5 viruses (from clades B and C). This
is the first demonstration of the induction by a candidate HIV vaccine
constructed from clade B laboratory strains of HIV of neutralizing
activity against R5 and clade C primary isolates. The data suggest
that, by virtue of their ability to induce cross-clade immune
responses, appropriately formulated HIV vaccines based on a finite
number of HIV isolates may ultimately be able to protect against the
wide range of HIV isolates affecting the populations of many geographic regions.
Progress in the development of an
effective vaccine for human immunodeficiency virus type I (HIV-1) has
been gauged in large part by the ability to elicit measurable
virus-specific CD8+ cytotoxic T lymphocytes (CTLs) and
neutralizing antibodies (Abs) as critical correlates of protective
immune responses (8, 29, 36). The major targets for
neutralizing Abs are gp120 and, to a lesser extent, the transmembrane
gp41 envelope glycoproteins of the virus (8). The first HIV
vaccines advanced to clinical trials were based on recombinant envelope
(Env) subunits derived from T-cell line-adapted (TCLA) strains of the
virus. While these vaccines generated neutralizing Abs with variable
and sometimes potent activity against the homologous TCLA HIV-1 vaccine
strain, CTL activity was generally poor against heterologous TCLA
strains (5, 25, 27, 41, 62) and the sera from vaccinated
volunteers failed to neutralize most primary isolates (28, 41,
42).
Since serum-neutralizing Abs are considered critical to protection
against most viral infections (58) and have been shown to
protect against HIV and simian immunodeficiency virus (SIV) infection
in several animal models (2, 6, 7, 11, 20, 38, 40, 60, 63, 68,
76), the ability to induce neutralizing Abs is thought to be an
important characteristic of candidate HIV vaccines. To be protective
against the many circulating subtypes of HIV, a vaccine will need to
induce broad neutralizing anti-HIV Abs against primary isolates, not
only TCLA clade B strains (1, 44, 56).
The current challenge for HIV vaccine design is to develop optimized
vaccines able to elicit both stronger cellular immune responses and
broader neutralizing responses against genetically diverse viral
species. One of the current strategies developed to induce both types
of immune responses is called the prime-boost strategy, using a live
poxvirus vector expressing the env gene of HIV-1 to prime
the immune system and a recombinant subunit HIV-1 envelope protein to
boost the immune response (13, 25, 26, 55, 73). Such
candidate vaccines have already been shown to induce both cellular and
humoral responses in animals (66, 67, 76), and a clade
B-based canarypox vaccine was shown to elicit cross-clade CTLs in
HIV-uninfected adults (19). However, the repertoire of
neutralizing Abs induced by these prime-boost protocols in most
volunteers was directed against the homologous TCLA strains from which
the vaccine was made, a limited number of heterologous TCLA HIV
strains, and a limited number of X4-tropic primary clade B viruses
(4, 12, 16, 17, 67, 74, 77). These initial results suggested
that this vaccine regimen induced a quite restricted humoral immune
response. To test this assumption, the Abs induced by such a
prime-boost regimen were tested for their ability to cross-react with
V3 peptides and recombinant gp160 proteins derived from viruses of
different clades and to neutralize viruses of different tropism from
several clades.
Subjects and specimens tested.
Twenty human sera were
obtained from the Division of AIDS (DAIDS), National Institutes of
Health, from participants in trials conducted by the AIDS Vaccine
Evaluation Group and sponsored by the National Institute of Allergy and
Infectious Diseases. Sera were obtained from HIV-uninfected volunteers,
18 to 60 years of age, of both sexes, who were enrolled in AIDS Vaccine
Evaluation Group protocol 029. This protocol consisted of an
accelerated prime-boost immunization schedule using recombinant
canarypox virus (vCP205 [Pasteur Mérieux/Connaught
Laboratories] expressing gp120MN, the transmembrane
anchoring region of gp41LAI, GagLAI, and a
portion of PolLAI) and rgp120SF2 in MF59
adjuvant (Chiron Corp, Emeryville, Calif.). HIV-uninfected subjects
were immunized intramuscularly at 0, 1, 2, and 3 weeks with vCP205,
boosted at 4 and 12 weeks with rgp120SF2, and bled 2 weeks
after the last boost. All reagents were administrated intramuscularly.
All sera were heat inactivated at 56°C for 30 min prior to use. The
panel of sera received from DAIDS included one HIV-positive serum (from the repository) and three HIV-negative sera (one from a volunteer in
the study who received placebo only and two from vaccinees bled prior
to immunization). All sera were shipped coded and tested blind. Two
additional known HIV-negative sera were used as negative controls, and
sera from HIV-positive patients from the Veterans Affairs Medical
Center (New York, N.Y.) (designated SX3, SX5, SX7, SX14, and SX16) were
used as known positive controls.
Peptides and recombinant proteins.
Fifty-three 19- to 30-mer
peptides which span the tip of the V3 loops were used; these were
derived from the sequences of seven clade A viruses, eight clade B
viruses, eight clade C viruses, eight clade D viruses, two clade E
viruses, six clade F viruses, six clade G viruses, three clade H
viruses, and five clade O viruses. The peptides were synthesized and
purified by standard procedures as described previously (75)
and purchased from Intracel, Inc. (Cambridge, Mass.), Genemed
Biotechnologies, Inc. (South San Francisco, Calif.), or Princeton
Biomolecules Corp. (Columbus, Ohio) or provided by A. Conley (Merck
Research Institute), C. Fiol (Colorado State University), or T. VanCott
or L. Loomis-Price (H. M. Jackson Foundation). None of the N- or
C-terminal amino acids were derivatized, and none of the peptides were cyclic.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
A Human Immunodeficiency Virus Prime-Boost
Immunization Regimen in Humans Induces Antibodies That Show Interclade
Cross-Reactivity and Neutralize Several X4-, R5-, and Dualtropic Clade
B and C Primary Isolates
ABSTRACT
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
INTRODUCTION
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
MATERIALS AND METHODS
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
Virus isolates. A total of 14 primary isolates from different clades were used, all being passaged exclusively in peripheral blood mononuclear cells. These included isolates HIV-1SF2 and HIV-1SF33 (both dualtropic [R5X4]), obtained from J. Levy (University of California at San Francisco), and isolate HIV-1MNp (X4), recently isolated by John Sullivan (University of Massachusetts Medical School, Worcester) from frozen spleen tissue from the patient from whom isolate HIV-1MN had been obtained. HIV-1MNp has never been passaged in cell lines. Isolates HIV-1JR-FL (R5), HIV-1SM993 (R5), HIV-192BR025 (R5), HIV-193BR029 (R5), HIV-193BR020 (R5X4), and HIV-193IN904 (R5) were supplied by the National Institutes of Health AIDS Research and Reference Reagent Program; isolates HIV-1CA4 (R5) and HIV-1CA20 (R5) were obtained from G. van der Groen (Institute of Tropical Medicine, Antwerp, Belgium); HIV-1BX08 (R5) was obtained from H. J. A. Fleury (Université de Bordeaux II, Bordeaux, France); and isolates HIV-1748 (X4) and HIV-12036 (R5X4) were obtained from D. Katzenstein (Stanford University, Stanford, Calif.).
ELISA.
A standard peptide enzyme-linked immunosorbent assay
(ELISA) was used (22, 23). Briefly, V3 peptides were coated
onto plastic Immulon 2HB plates at 1 µg/ml. Plates were blocked for 2.5 h at 37°C with 7.5% fetal calf serum and 2.5% bovine serum albumin in phosphate-buffered saline (PBS) and then washed four times
with PBS containing 0.05% Tween 20 (pH 7.4). Subsequently, 50 µl of
each serum, at a dilution of 1:100, was added to each well for 1.5 h at 37°C. After washing, the plates were incubated with alkaline
phosphatase-conjugated goat anti-human immunoglobulin G (
-chain
specific), color was developed with p-nitrophenyl phosphate, and plates were read at 410 nm. Negative controls consisted of V3-coated wells reacted with known HIV-negative sera. Sera from five
known HIV-positive subjects from New York were introduced into this
assay as positive controls for clade B infection. For ELISAs with
recombinant proteins, the plates were coated with 0.5 µg of
recombinant protein/ml following the same protocol.
Neutralization assay. The GHOST cell neutralization assay was used (9). GHOST-X4 cells were used as target cells in assays with X4 and dualtropic viruses. GHOST-R5 cells were used with the R5 viruses. The GHOST cells were maintained in Dulbecco's modified Eagle's medium supplemented with 10% fetal calf serum, 1% glutamine, 2% penicillin and streptomycin, plus 500 µg of geneticin, 50 µg of hygromycin, and 1 µg of puromycin per ml. Cell monolayers, when confluent, were resuspended using 0.25% trypsin. The cells were carried for 15 passages and then replaced with fresh cells from stocks frozen at the second or third passage.
For the GHOST cell neutralization assay, 6 × 104 GHOST cells/well per 0.5 ml were seeded into wells of 24-well tissue culture plates and allowed to grow for 24 h. Each virus stock was diluted to a predetermined concentration which had been found to result in ~1,000 infected cells per 15,000 total cells measured cytofluorometrically at the end of the assay. Equal volumes of appropriately diluted virus and heat-inactivated serum at a 1:10 dilution were mixed and incubated at 37°C for 1 h before being applied to the GHOST cells in the presence of DEAE-dextran at 8 µg/ml. After overnight adsorption, the virus- and Ab-containing medium was removed, the cell monolayers were washed, and the cells were incubated for 3 to 4 days. For harvest, cells were resuspended using 1 mM EDTA, fixed in 2% formaldehyde, and then analyzed using a FACScan flow cytometer (Becton-Dickinson). The percent neutralization was calculated using the number of infected cells observed in the absence of human serum as the denominator. Two known HIV-negative human sera were used as negative controls in each experiment.| |
RESULTS |
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Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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Reactivity of anti-V3 loop antibodies.
The coded panel of sera
and the known HIV-positive sera were tested for cross-reactivity to V3
peptides derived from the sequences of viruses of group M (clades A
through H) and group O. Results from each serum-peptide combination are
shown in Fig. 1. For clarity, the optical
density (OD) values have been represented as a spectrum of colors
corresponding to the degree of reactivity observed.
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Reactivity with recombinant HIV envelope proteins.
Cross-clade
reactivity to the entire envelope was then tested. The availability of
such molecules in recombinant form was limited. All that were obtained
(six from clade B strains, two from clade D strains, and one from a
clade E strain) were tested. All vaccinees' sera reacted strongly with
rgp120SF2 and rgp120MN, which were both
homologous to the immunizing antigens (Fig.
2). Strong reactivity to
rgp160IIIB was also detected. Vaccinees' sera also showed
significant reactivity with the heterologous rgp120 and rgp160
molecules from primary isolates of other clade B, D, and E strains.
This cross-reactivity was not due to anti-gp41 antibodies, as shown by
the weak reactivity of vaccinees' sera with gp41 (Fig. 2). Indeed, it
has previously been shown that without a gp120 boost, priming with
recombinant virions produces little antibody activity (76),
and this would account for the paucity of anti-gp41 Abs in the
vaccinees' sera tested here. While vaccinees' sera reacted with all
of the recombinant envelope molecules tested, the levels of Abs
detectable in the HIV-positive sera against six of eight rgp120 and
rgp160 molecules derived from clades B, D, and E were comparable to or
higher than those detected in the vaccinees' sera (Fig. 2).
Interestingly, reactions were detected with rgp160 of clade E even
though no reactivity was noted against any V3 peptides from clade E.
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Neutralization of primary isolates by vaccinees' sera.
Binding of Abs to recombinant proteins and peptides of HIV has
previously been shown not to be predictive of primary isolate neutralization (69, 71), and this appears to be
substantiated by the data presented below. Thus, the capacity of the
vaccinees' sera to neutralize 14 HIV-1 primary isolates was tested
using the GHOST cell neutralization assay. Ten primary isolates from clade B were previously tested in this assay (9).
Neutralization curves showed that for the primary isolate
HIV-1SF2, the maximum level of neutralizing activity (70%)
of several HIV-1-positive sera with broad reactivity was maintained
through a dilution of 1:40 and gradually decreased to 50%
neutralization at a dilution of 1:500 and to 25% neutralization at a
dilution of 1:1,000 (9). Furthermore, the various primary
isolates differed in their capacity to be neutralized by HIV-positive
sera, displaying 50% neutralizing titers ranging from 1:20 to 1:5,000.
Therefore, for our study, HIV-1-positive sera as well as vaccinees'
sera were tested at a dilution of 1:20. Significant neutralization was
defined on the basis of the 95% confidence limit of the percentage of
neutralization by HIV-negative sera (shown as the shaded area in Fig.
3). This was established on the basis of
54 assays using five HIV-negative sera (at a final serum dilution of
1:20) and the 14 primary isolates. Thus, significant neutralization is
depicted when the percent neutralization is above the shaded area in
Fig. 3 (>23%). Two HIV-1-positive sera (SX5 and SX16; see Fig. 1)
were used as positive controls. The sera from these two HIV-positive
individuals had previously been found to neutralize a large majority of
primary isolates from clades B and C in the same assay (data not
shown); the percent neutralization obtained with these HIV-positive
sera is indicated in red symbols in Fig. 3.
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). The mean percent neutralization
for each virus strain is indicated by a black line (vaccinees' sera)
or by a red line (HIV-positive sera). The GHOST cell neutralization
assay was used (
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DISCUSSION |
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Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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It is currently assumed that both a vigorous HIV-specific CTL response and serum neutralizing activity against primary HIV isolates will be important immune responses induced by a preventive HIV vaccine. To date, the prime-boost regimen, using recombinant canarypox virus vaccine constructs and recombinant envelope subunits, has most successfully induced both of these HIV-specific immune responses. This regimen was able to elicit cross-clade CTL reactivities (19) but was thought to have induced only a very restricted humoral response. In fact, these prime-boost protocols were shown to induce a variety of immunochemically reactive Abs, including Abs mediating Ab-dependent cell-mediated cytotoxicity and Abs that neutralize autologous TCLA strains but relatively few primary isolates of clade B (12, 74, 77). However, while cross-clade CTL activity was studied and demonstrated, as mentioned above, no study of cross-clade primary isolate neutralizing activity has been reported. This led to a tacit assumption, in the absence of data, that cross-clade neutralizing activity has not been and cannot be induced by TCLA clade B-based vaccines.
The experiments presented here investigated the nature of the Ab repertoire in vaccinees' sera following immunization of healthy seronegative volunteers with a prime-boost vaccine regimen derived from TCLA clade B HIV-1MN and HIV-1SF2 isolates. The data demonstrate that vaccine-induced Abs are not strain or even clade B specific, but rather are broadly cross-clade reactive. The sera showed the strongest and most extensive immunochemical reactivity with V3 peptides from clades B, C, and F. In contrast, none of the vaccinees' sera bound to V3 peptides from clade E and group O. These results extend previous studies describing (i) the extensive cross-clade reactivity of human anti-V3 serum and monoclonal Abs (3, 10, 21, 23, 47, 50, 57, 75), (ii) the similarity of clade A and C V3 loops and of clade B and F V3 loops, and (iii) the divergence of the clade D V3 loop, based on serologic and sequence data (3, 35, 57). The lack of reactivity of vaccinees' sera with the clade E and group O V3 peptides is also consistent with previous serological and functional analyses of Ab activity (39, 43, 49). Furthermore, vaccinees' sera were able to bind to gp160 glycoproteins of primary isolates of HIV-1 subtypes B, D, and E. These results are consistent with recent data showing that Abs induced by MN and IIIB recombinant gp120 HIV-1 vaccines were able to bind to oligomeric native HIV-1 envelope glycoproteins of primary isolates of HIV-1 from clades A, D, and E measured by a flow cytometric indirect immunofluorescence assay (24).
Studies of the neutralization of X4, R5, and dualtropic viruses and of viruses from clades B, C, and F also demonstrated broader reactivity of vaccinees' sera than had previously been documented or anticipated. While the breadth of neutralizing activity induced by immunization with a clade B, TCLA-based vaccine is narrower than that induced by infection with clade B strains, vaccinees' sera displayed neutralizing activity against X4, R5, and dualtropic primary isolates, and significant neutralizing activity was found in 18 of 20 vaccinees' sera against an R5 isolate of clade C. Whether this activity is protective cannot be ascertained without phase III efficacy studies; however, it is noteworthy that passive immunization studies conducted in chimpanzees, macaques, and SCID-hu mice suggest that Ab alone can be protective against HIV and SIV challenge (15, 53, 61) and that, in the case of other viral infections, such as polio and hepatitis B, vaccine-induced Ab titers as low as 1:4 are sufficient to confer protection (18, 31, 52, 64, 65).
Significant neutralizing activity in vaccinees' sera was demonstrated in 45% of the 257 virus-serum combinations tested; this compares favorably with studies of sera from HIV-positive subjects in which 65% of 224 combinations of virus and serum (51), 56% of 107 combinations (72), and 52% of 441 combinations (48) were found to have neutralizing activity. The overall neutralizing activity was, however, weaker in the vaccinees' sera than in the HIV-positive sera and cannot be defined as broad. Nevertheless, these data constitute the first proof of the principle that a clade B, TCLA (X4)-based candidate HIV vaccine can induce detectable neutralizing activity against viruses from a heterologous, R5 phenotype and against a heterologous clade. These data also suggest that the potential protective capacity of vaccines may not be restricted to a single clade. However, it also appears that protection may not be conferred against all viruses belonging to the clade from which a single immunogen is derived. The spectrum of protection may turn out to be more closely related to immunologically defined groups (immunotypes) than to genotypically defined groups (clades), a concept that is supported by several other published studies (50, 72, 75).
Our data suggest that an HIV vaccine, in order to confer truly broad protection, will most probably need to include a mixture of immunogens representative of the different immunologic groups of HIV. Quite possibly not all immunologic groups of HIV will be required as components of such a polyvalent vaccine, since components from a single virus or immunotype are able to induce cross-reactivity to heterologous viruses. This is the case with the monovalent influenza virus vaccine, for example, which is able to induce cross-reactive Abs (32, 37). Similarly, vaccines against bacterial pathogens require a limited number of serotypes to protect against a wide number of immunologic variants: in the case of pneumococcal vaccines, components from approximately 23 common serotypes confer immunity to more than 80 serotypes of Streptococcus pneumoniae (59). Thus, for HIV, the challenges presented to vaccine development against a virus family with extreme genetic variation may be addressed successfully by the ability of the immune system to recognize related, conserved structures and conformations defining antigenic variability which might be less extreme than the well-documented variation in the sequences of HIV.
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ACKNOWLEDGMENTS |
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This study was supported in part by grants from the National Institutes of Health (R01-AI 32424, R01-AI 36085, R01-HL 59725, and P01-AI 27742 [which supports the Immunology and Flow Cytometry Cores of the NYU Center for AIDS Research]) and from the Department of Veterans Affairs (Research Center for AIDS and HIV Infection and Merit Review funding).
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FOOTNOTES |
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* Corresponding author. Mailing address: c/o VA Medical Center (Room 18124N), 423 E. 23rd St., New York, NY 10010. Phone: (212) 951-3211. Fax: (212) 951-6321. E-mail: zollas01{at}popmail.med.nyu.edu.
Present address: Henry M. Jackson Foundation, Rockville, Md.
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Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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