Human Monoclonal Antibodies that Neutralize HIV-1
Miroslaw K. Gorny1
- Susan Zolla-Pazner
The HIV Immunology Database provides continuously updated information on
monoclonal antibodies (mAbs) against HIV-1 produced by various
techniques, including cellular methods utilizing Epstein-Barr
transformation, phage display technology, antigen stimulation of
lymphoid cells in vitro, and preparation of hybridomas from cells of
transgenic mice. In this review, particular attention is focused on
those human mAbs that are able to inhibit the infectivity of HIV
virions. These mAbs target several clusters of neutralizing
epitopes in the HIV-1 envelope proteins, including V1, V2, V3,
CD4bs, CD4i in gp120, and cluster I, cluster II, and a region
adjacent to cluster II in gp41. Only five of the 174 mAbs listed
here can be classified as broadly and potently neutralizing for
HIV-1 primary isolates; these include mAbs 2G12, IgG1b12, and
447-52D (specific for gp120) and 2F5 and 4E10 (specific for gp41).
Certain other monoclonal reagents are capable of broad
neutralization as Fab fragments but not as IgG molecules. The
existence of human mAbs with neutralizing activity against diverse
HIV-1 isolates demonstrates the ability of the human immune response
to recognize B cell epitopes on the HIV-1 envelope that are shared
and that, when complexed with antibody, prevent virus infectivity.
The paucity of such broadly neutralizing mAbs highlights the
challenge faced by designers of HIV-1 vaccines: to design a vaccine
that will induce that small proportion of antibodies with broad
The HIV Immunology Database catalogues existing rodent and human
monoclonal antibodies (mAbs) that are specific for various proteins
of HIV-1. The human mAbs, which are reviewed herein, were produced by
a variety of different techniques, although the two techniques that
have given rise to the majority of useful mAbs are based on hybridoma
and recombinant technologies. Both techniques have resulted in
extremely valuable mAbs that have provided important information
about the antigenic structure of neutralizing epitopes. Hybridoma
techniques are based on the transformation of B cells from the cells
of infected individuals (Gorny1989), and the mAbs derived
from these cells represent antibodies that are part of the normal
human B cell repertoire. In contrast, while the recombinant
technology has several advantages over the cellular technology
(Barbas1992), given the random recombination of heavy and light
chains that takes place in vitro during this process, the resulting
Fab fragments and IgG molecules may not actually represent antibodies
that exist in human hosts (Huang2004).
The 174 mAbs summarized in this review are grouped on the basis of the
epitopes that they recognize in gp120 and gp41. Among these mAbs and
Fab fragments, 11 regions are recognized, however, only five human
mAbs specific for four regions of gp120 and gp41 have been established
as capable of broad and potent neutralization of HIV-1; these include
mAbs 2G12, IgG1b12, and 447-52D (specific for various epitopes in
gp120) and 2F5 and 4E10 (specific for gp41). Thus, while the
existence of these latter mAbs demonstrates that the human immune
system has the capacity to recognize shared neutralizing epitopes on
the HIV-1 envelope glycoproteins, the paucity of broadly neutralizing
mAbs highlights the limited immunogenicity and/or restricted
availability of the regions in the native virions that are critical
for virus infectivity.
Several phenomena may explain the rarity of functional antibodies
against regions of the virus that are indispensable for its
infectivity. These include, but are not limited to, the following:
(a) the ability of the virus to continually vary its sequence in
critical regions while maintaining function (Zolla-Pazner2004a);
(b) carbohydrate masking of critical epitopes (Wei2003,Back1994); (c) conformational masking of receptor-binding sites
(Kwong2002); (d) poor immunogenicity of some neutralizing
epitopes (Trkola1996b); and (e) inaccessibility or transient
exposure of neutralizing epitopes on the intact virus and on the virus
as it binds to cell receptors.
Despite these phenomena, which form the basis for virus escape from
the neutralizing potential of antibodies, the human humoral immune
response is able to produce antibodies that neutralize HIV-1. The
characterization of neutralizing epitopes recognized by human mAbs
provides the basic data for the rational design of effective vaccine
immunogens. In addition, the identification and characterization of
neutralizing human mAbs may provide reagents for passive immunization
to prevent infection, as in the setting of maternal-fetal
transmission. These mAbs should also provide important information
about mechanisms of virus neutralization, the antigenic structure of
the virus, and the nature of the B-cell repertoire that can be tapped
to provide protective humoral immune responses against the virus.
The characteristics of 174 human mAbs that target the envelope
glycoproteins of HIV-1 are reviewed below. The epitopes within gp120
and gp41 that are recognized by these mAbs have been mapped and are
catalogued in the HIV Immunology Database. For the convenience of the
reader, we have linked the mAbs discussed in this review with each
antibody's web page in the HIV Immunology Database
No anti-V1 mAbs have been derived from the cells of infected humans.
However, the HIV Immunology Database provides information on ten human
anti-V1 mAbs (Table 1
) that were generated from
transgenic mice carrying the genes coding for fully human IgG κ.
``xeno-mAbs'' were derived from transgenic mice that had been
immunized with native recombinant gp120 from
the Ab-producing cells were selected with
). All of these
anti-V1 xeno-mAbs display potent type-specific neutralizing activity
against the autologous strain SF162 with 50% neutralizing doses
(ND50) in the range of 0.3 to 4.5 µg/ml, as determined in a
luciferase assay. Ten out of the 35 xeno-mAbs selected with
were specific for V1, suggesting that in
this transgenic model, V1 is an immunodominant epitope (He2002
The dearth of human anti-V1 mAbs derived from the cells of infected
humans is probably related to the very high diversity of the V1
domain; this would render the selection of anti-V1 mAbs with
heterologous gp120 reagents a difficult task. However, the lower
immunogenicity of this region in the setting of natural infection
cannot be excluded.
Anti-V2 antibodies have the capacity to neutralize HIV, but their
activity is generally weak and their cross-reactivity is usually
limited, suggesting that the antibodies with this specificity may have
limited utility in mediating vaccine-induced, broad-based protection.
The HIV Immunology Database contains a list of five anti-V2 human
mAbs, two Fab fragments generated from HIV-infected individuals, and
one xeno-mAb (Table 2
). The most thoroughly analyzed of
the anti-V2 mAbs, mAb 697-D, could only weakly neutralize three of
four primary isolates when a relatively high dose of mAb was used
against a low virus input (Gorny1994
); this mAb displayed no
neutralizing activity against four TCLA strains
). mAb 697-D recognizes a conformational
epitope, showing only weak reactivity with a V2 peptide; it binds
weakly and only sporadically to intact virions from clades A, B and D
); similarly, other human anti-V2 mAbs, such as mAbs
830A, 1357, 1362 and 1393A, could bind to soluble gp120 but showed
only weak and sporadic binding to virions of primary isolates, with
the most frequent binding to B, C and D clades (Nyambi2000
). mAb 697-D could not inhibit the ability of gp120 to
block the binding of MIP-1 beta to CCR5, suggesting that the V2 region
does not block envelope/coreceptor interaction (Trkola1996a
Two Fab fragments, L15 and L17, are specific for the V2 domain
four Fab fragments, L25, L39, L40 and L78, are directed to complex
epitopes that include the V2 loop and the CD4 binding site (CD4bs)
). These latter Fab fragments
were retrieved after epitope masking of gp120 with CD4bs Fab fragments
during the screening stage. They were characterized by their V2
region-dependence, indicated by their sensitivity to amino acid
changes in the V2 loop and by competition with murine anti-V2 mAbs. In
addition, they are sensitive to amino acid changes usually associated
with CD4 binding, and their binding to gp120 can be inhibited by
soluble CD4. Among these several Fab molecules, only L25 and L78
mediate weak neutralization of T cell line-adapted (TCLA) viruses;
neutralizing activity against primary isolates was not reported. The
poor performance of these anti-V2 and anti-V2/CD4bs Fab fragments in
neutralization assays does not exclude the possibility that, as whole
IgG molecules, they could display neutralizing activity since Fab
fragments usually display affinities that are lower by two to three
orders of magnitude than intact IgG molecules. However, no studies of
these fragments as whole IgG molecules have been published, and the
lack of potent neutralizing activity by anti-V2 IgG mAbs (see above)
is not an encouraging indicator.
In summary, the information about anti-V1 and anti-V2 mAbs is
incomplete because the number of mAbs, Fab fragments and xeno-mAbs is
still relatively small. The results utilizing these mAbs suggest that
anti-V1 mAbs are rather type-specific but can be quite potent, while
anti-V2 are more broadly neutralizing but of low activity. A notable
exception is the chimp mAb C108G, which is directed against a
glycan-dependent epitope localized in V2 and was shown to neutralize
primary HIV-1BaL isolate and TCLA strain IIIB (Vijh-Warrier1996).
||IgM mAb, in vitro stimulation
Human antibodies directed to the V3 loop of gp120 constitute the major
group of human mAbs in the database. There are currently 33 IgG mAbs,
two Fab fragments generated from HIV-infected individuals, four
xeno-mAbs produced by transgenic mice, and three IgM mAbs produced by
in vitro stimulation of peripheral blood mononuclear cells (PBMC) with
V3 peptides (Table 4
). These numbers reflect both the
strong immunogenicity of the V3 region and the early interest in
anti-V3 Abs generated when it was shown that they could neutralize
TCLA virus strains (Rusche1988
); subsequent studies have
documented the ability of anti-V3 antibodies to also neutralize
primary isolates (Scott1990
and to mediate protection as demonstrated in passive immunization
experiments in various animal models (Emini1992
Many of the human anti-V3 mAbs were produced from cells of
HIV-infected individuals who had been infected for several years;
these were shown to neutralize TCLA and/or primary isolates
(Scott1990,Gorny2004,Gorny1993,Gorny1997,Gorny2002,Moore1995). In contrast, the IgG anti-V3 xeno-mAbs displayed
neutralizing activity that appeared to be specific for the
immunizing SF162 virus strain (He2002), while the IgM mAbs that
were induced in vitro by antigenic stimulation of cells from
HIV-uninfected individuals displayed no neutralizing activity
(Ohlin1992). These results suggest that the induction of
broadly reactive and potent anti-V3 antibodies may require prolonged
antigenic stimulation, resulting in mature and broadly reactive
anti-V3 antibodies. This is consistent with the slow appearance of
broadly reactive antibodies in the sera of infected individuals
(Pilgrim1997), a factor that could have profound implications
for the development of vaccine regimens.
Another important element in the generation of broadly reactive and
potent human anti-V3 mAbs is the method used to select for cells
producing the appropriate mAbs. Although the most broadly reactive of
the neutralizing anti-V3 mAbs, 447-52D, was selected using a V3
peptide, the majority of mAbs selected with V3 peptides do not
efficiently neutralize primary isolates (Gorny1993). This is
most probably due to the fact that peptides are highly flexible and
may assume a myriad of conformations. Thus, most of the V3 mAbs
selected with peptides are directed to structures which are irrelevant
in the context of primary isolate infectivity; by chance, the
structure of the V3MN
peptide that captured mAb 447 bore a relevant
conformation. In contrast, the use of a V3 fusion protein for mAb
selection in which the V3 region retains a structure which
approximates that of the native V3 loop (Kayman1994) resulted in
the identification of mAbs that recognize conformation-sensitive V3
epitopes; the majority of these latter anti-V3 mAbs neutralize many
primary isolates (Gorny2002). Thus, within the repertoire of
anti-V3 antibodies elicited in HIV-infected subjects, there are
broadly reactive neutralizing antibodies, and these can be rescued if
appropriate selection methods are employed.
The conformation-sensitive anti-V3 mAbs can neutralize primary
isolates, and most can cross-neutralize a variety of isolates from
clade B and, to a lesser extent, those from other clades
(Gorny2004,Gorny2002). The mAb 447-52D, though selected with
a peptide, recognizes a conformational determinant (Sharon2003,Stanfield2004,Gorny2002),
and it is the most broadly neutralizing of all the currently
existing anti-V3 mAbs. This mAb interacts with the 14 residues at
the crown of the V3 loop; its ``core epitope'' is defined by the
sequence GPxR, a motif that is highly conserved among clade
B viruses and which exists in a minority of other HIV subtypes
(Gorny1992). The presence and
recognition of the arginine (R) residue in the core epitope
is required for mAb 447-52D to exercise its activity
(Zolla-Pazner2004b)), a fact that is explained by structural
studies of this mAb in complex with a V3 peptide showing salt bridge
and cation-pi interactions formed between the R residues in
the core epitope and residues in
the heavy chain of the mAb (Stanfield2004). Other anti-V3
mAbs, such as mAbs 2182, 2191, 2219, 2412, 2442 and 2456
(Table 4), do not recognize the same epitope as
447-52D, yet also display the ability to cross-neutralize primary
isolates (Gorny2004,Gorny2002). This cross-reactivity reveals
the presence of features within the V3 loop which are conserved
despite the sequence variation in this region. This structural
conservation is also reflected in the role of the V3 loop in binding
to the chemokine receptors which act as coreceptors for the virus
The HIV Immunology Database provides information about 30 anti-CD4bs
human mAbs and 15 recombinant Fab fragments generated from PBMCs or
bone marrow of HIV-1-infected individuals. In addition, there are six
human anti-CD4bs mAbs listed which were produced from the cells of
transgenic mice (Table 5
). Antibodies specific to the
CD4bs inhibit the binding of sCD4 to gp120 and, as a consequence,
interfere with virus attachment to the target cells. The CD4bs is
made up of residues from C2, C3 and C4, conferring the conserved
character of this domain and explaining the cross-reactivity of
anti-CD4bs mAbs when tested for their ability to bind to gp120
molecules from viruses of diverse subtypes (Jeffs2001
immunochemical cross-reactivity is reflected in the ability of these
mAbs to neutralize a broad array of TCLA strains; surprisingly,
however, most anti-CD4bs mAbs cannot neutralize primary isolates
). Since the CD4bs is a
key feature of both TCLA and primary isolates, the selective
neutralization of TCLA strains as opposed to primary isolates by most
anti-CD4bs mAbs is surprising and still not fully explained. MAb
IgG1b12 is a striking exception to the generalization that anti-CD4bs
do not neutralize primary isolates (Burton1994
). Indeed, this
mAb neutralized half of 90 primary isolates from diverse subtypes, and
when tested against 30 primary isolates of subtype B, it neutralized
The differential activity of IgG1b12 vs. other anti-CD4bs mAbs has
not been fully explained. It is possible that IgG1b12, which was
produced using recombinant technology (Barbas1992), possesses a
paratope that does not exist in nature. There is, however, nothing
notably unusual about the structure of this mAb (Saphire2001).
Other explanations for its broad and potent activity may lie in its
unusual dependence on regions within the V2 domain in order for
binding to occur. Thus, it was shown that the Fab fragment of b12, as
opposed to that of other anti-CD4bs mAbs, has reduced binding activity
to V2-deleted gp120, and that deletion of V2 from isolate SF162, but
not of V1, diminished the neutralizing activity of IgG1b12 for this
virus; this distinguished IgG1b12 from another anti-CD4bs mAb, 654-D,
and from IgG-CD4 (Stamatatos1998). Additional evidence that the
IgG1b12 epitope includes a portion of V2 comes from data showing that
escape mutants generated when JR-FL was cultured in the presence of
IgG1b12 displayed two substitutions in V2 as well as one in C3
(Mo1997). The specificity of IgG1b12 for the CD4bs and V2 is
reminiscent of the ``V2/CD4bs'' Fab fragments described by Dietzl
et al. (Ditzel1995,Ditzel1997) (see above); however, no
primary isolate neutralizing activity has been described for these
latter Fab fragments, nor have they been compared to IgG1b12 in any
A notable feature of mAb IgG1b12 is its long CDR H3 region, consisting
of 18 amino acids. The CDR H3 projects above the rest of the
antigen-binding site of the mAb, fitting into the pocket of the CD4bs
of gp120 (Saphire2001). Interestingly, several other broadly
reactive and potent neutralizing human mAbs, such as anti-V3
mAb447-52D (see above), anti-CD4i mAbX5 (see below) and anti-gp41 mAb
2F5 (see below), also have long CDR H3 regions consisting of 20 to 22
residues (Darbha2004,Kunert1998,Stanfield2004), a
characteristic that is shared by many human anti-viral Abs
This is a small group of human mAbs (Table 6
binds to the gp120 bridging sheet, a beta-sheet consisting of four
anti-parallel beta-strands contributed by the C4 region and the V1/V2
Several anti-CD4i mAbs were derived by Epstein-Barr virus
transformation of B cells from the PBMCs of HIV-infected subjects
(Thali1991,Xiang2002), while Fab X5 was selected from a phage
display library derived from an HIV-1 infected donor whose serum
displayed strong neutralizing activity (Moulard2002). The
phage library was screened with gp120-CD4-CCR5 complexes which
exposed the CD4i epitope. The X5 epitope is near the CD4bs and CCR5
binding site but does not overlap with them; its specificity is
slightly different than the 17b epitope which reacts with the CCR5
binding site only (Darbha2004,Moulard2002). Immunochemical
analyses show that the CD4i epitope only becomes accessible after
the binding of gp120 to CD4. For example, anti-CD4i mAbs have little
or no ability to bind to gp120 in ELISA until the envelope protein
is preincubated with sCD4, which, by definition, induces the
conformational changes that expose the CD4-induced epitope.
Since the bridging sheet interacts with the chemokine receptors, the
mechanism of neutralization of the anti-CD4i mAbs is thought to be
through the inhibition of gp120 binding to CCR5 and CXCR4
(Trkola1996a). However, the anti-CD4i mAbs display no
neutralizing activity against primary isolates. Only the Fab or
single chain forms of antibodies with specificity for the CD4i epitope
display neutralizing activity (Labrijn2003). Thus, the scFv and
Fab fragments of mAbs 17b and 48d displayed more potent neutralizing
activity against JR-CSF, JR-FL and ADA than did the intact IgG forms
of these mAbs, and, similarly, the scFv and Fab fragments of X5
potently neutralized these viruses but lost this activity when
converted into a whole IgG molecule (Labrijn2003). These data
suggest that the size of the neutralizing molecule is a critical
factor, and models juxtaposing the gp120 molecule on the virus
particle and the chemokine receptor on the surface of the target cell
indicate that the bulk of an intact IgG molecule prevents its
insertion between gp120 and the coreceptor (Labrijn2003,Dey2003,Moulard2002). Thus, steric hindrance precludes the ability of
anti-CD4i IgGs from effectively neutralizing virus infectivity.
Nevertheless, the X5 Fab neutralizes primary isolates from clades A,
B, C, D, E, F and G, and neutralizes R5, X4 and R5X4 isolates, showing
the exceptionally conserved character of CD4i epitopes
There is only one neutralizing human mAb, 2G12, which recognizes an
epitope composed of carbohydrates (Table 7
); this mAb is specific for
high-mannose and/or hybrid glycans at residues 295, 332 and 392 with
peripheral glycans from 386 and 448 on either flank (Sanders2002
). These carbohydrate moieties are located on an exposed
surface of the gp120 trimer that does not interact with CD4 or the
chemokine receptors. Nonetheless, mAb 2G12 inhibits gp120 interaction
with CCR5 as shown in MIP-1beta-CCR5 competition studies
). These data led to the hypothesis that
the neutralizing activity of mAb 2G12 is an indirect, steric effect
manifested by a binding site that is physically close to the
receptor-binding sites of gp120 (Scanlan2002
). mAb 2G12 potently
neutralizes TCLA and was recently shown to neutralize 41% of primary
isolates representing various subtypes (Binley2004
Despite the standard cellular technique used in the generation of mAb
2G12 and the commonly employed approach for selection of the mAb by
measuring binding to gp160 (Buchacher1994), mAb 2G12 is unique
both in terms of structure as well as specificity. Recent
crystallographic studies revealed that two Fabs of mAb 2G12 assemble
into an interlocked VH domain-exchanged dimer forming an extended
binding site which targets the aforementioned conserved cluster of
oligomannose moieties on the surface of gp120 (Calarese2003).
The 2G12 epitope is poorly immunogenic as reflected by competitive
binding assays that demonstrated that 2G12-like antibodies were absent
from all of 16 sera from HIV-infected long-term survivors and AIDS
patients (Trkola1996b). These factors--the unusual structure of
mAb 2G12, its unusual epitope, and the poor immunogenicity of this
epitope--suggest that, despite the undeniable potency and breadth of
activity of mAb 2G12, the probability of inducing similar Abs with a
vaccine may be quite low.
|Adjacent to Cluster II*
* Cluster I: aa 596-613; Cluster II: aa 644-663; Adjacent to
Cluster II: aa 662-676; Cluster III: conformational epitope
involving aa 619-648.
As shown in Table 8
, there are 28 human mAbs and 24
Fab fragments directed to the highly immunogenic regions of gp4
). Twenty-four mAbs and Fab fragments are
directed to the most immunodominant region, cluster I (aa 579-604),
19 mAbs and Fab fragments are specific for cluster II (aa
644-663), three are specific for an epitope adjacent to cluster
II, and six Fab fragments are specific for cluster III (a
conformational epitope involving aa 619-648). Only four out of
these 52 mAbs and Fab fragments have documented neutralizing
activity: mAbs 2F5, 4E10, clone 3 and Fab fragment Z13.
MAb 2F5 is one of the best studied of the human mAbs. It has broad
and potent activity, neutralizing 67% of 90 isolates from various
virus subtypes (Trkola1995,Binley2004,Burton2004). The linear
2F5 epitope is located near the transmembrane domain at aa 662-667, a
region which is adjacent to cluster II and is not well exposed on the
virus or on virus-infected cells (Sattentau1995,Nyambi1998,Ofek2004).
Immunochemical data show that 2F5 reacts strongly with peptide C43
representing a portion of the C-heptad repeat region of gp41, while
there is no reactivity with peptide N51, the N-heptad repeat region of
gp41. While mAb 2F5 reacts with the N51:C43 complex, which forms a
coiled-coil complex, it reacts with the complex less strongly than it
does with C43 alone (Gorny2000,deRosny2004). While this might
suggest that 2F5 interferes with the formation of the gp41
coiled-coil, this was not borne out by recent studies
(deRosny2004). Thus, the mechanism of neutralization by mAb 2F5
is still unknown, although interference with the late fusion process
has been suggested (deRosny2004).
MAb 4E10 and Fab Z13 are also specific for a region that is adjacent
to cluster II. They recognize the same epitope, and both are specific
for a predominantly linear and relatively conserved epitope at aa
671-677 that is proximal to that of 2F5 (Zwick2001). mAbs 4E10
and Z13 neutralize primary isolates of diverse clades, including A, B,
C, D and E (Zwick2001). While mAb 4E10 is the most broadly
neutralizing mAb currently described, it is less potent than the other
well-described, broadly neutralizing mAbs (Zwick2001,Binley2004,Burton2004).
MAb clone 3 binds to a linear epitope between aa 597 and 606 at the
C-terminal end of cluster I, the most immunodominant region of gp41
(Cotropia1996). The epitope is quite conserved, a fact
reflected by its ability to neutralize three diverse TCLA viruses
from clade B and three primary isolates from group O
(Ferrantelli2004,Cotropia1996). Beyond the activity of
clone 3 against these viruses, few details are known about its
functional breadth. The clone 3 epitope overlaps with the epitope
of mAbs 246 and 240 (aa 590-597 and 592-600, respectively).
Interestingly, these latter mAbs bind to cluster I but have little
or no neutralizing activity (Hioe1997) despite their ability to
bind to intact virus particles (Nyambi1998).
As noted above, the mechanism(s) of neutralization of all four
neutralizing anti-gp41 mAbs is still unknown. An indication that at
least some anti-gp41 mAbs may interfere with virus/cell fusion was
provided by studies of the fusion process at a suboptimal temperature
(31.5°C), which prolongs the time during which fusion
intermediates are exposed to mAbs (Golding2002). These
experiments showed that human mAbs against cluster II (mAbs 98-6, 1281
and 167-D) strongly inhibited fusion between HIV envelope-expressing
effector cells and target cells expressing appropriate receptors
Among the 174 human mAbs summarized in
Tables 1-8, only five mAbs (2G12,
IgGb12, 447-52D, 2F5 and 4E10) and two Fab fragments (X5 and Z13) can
be classified as broadly and potently neutralizing for HIV-1 primary
isolates. Presently, the epitopes targeted by some of these mAbs do
not appear to be practical targets for vaccine development due to
their weak immunogenicity (2G12, 2F5) or their inaccessibility to
antibody molecules (17b, X5, etc.). The CD4bs, which would appear to
be an ideal target for neutralizing antibodies, induces antibodies
which, for the most part, have little or no activity against primary
isolates. And, while the epitopes recognized by neutralizing V3 mAbs
are accessible and immunogenic, they induce a spectrum of antibodies
ranging from narrowly to broadly cross-reactive, but the latter
apparently require prolonged antigenic stimulation to emerge.
While the search for and design of effective immunogens continues, the
most efficacious of the mAbs described to date may serve as beacons to
illuminate the effort. Meanwhile, continuing work is needed, using
new screening techniques, to identify neutralizing mAbs to additional
classes of epitopes in order to provide the maximum number of viral
determinants to target with a vaccine.
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- Miroslaw K. Gorny1
- Department of Pathology, New York
University School of Medicine, New York, NY 10016
- Susan Zolla-Pazner2
- The Veterans Affairs New York
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