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Blood, Vol. 93 No. 6 (March 15), 1999:
pp. 1851-1857
Human Immunodeficiency Virus Replication Induces Monocyte Chemotactic
Protein-1 in Human Macrophages and U937 Promonocytic Cells
By
Manuela Mengozzi,
Camilla De Filippi,
Pietro Transidico,
Priscilla Biswas,
Manuela Cota,
Silvia Ghezzi,
Elisa Vicenzi,
Alberto Mantovani,
Silvano Sozzani, and
Guido Poli
From the AIDS Immunopathogenesis Unit, DIBIT, San Raffaele Scientific
Institute, Milano; the Department of Immunology and Cell Biology,
"Mario Negri" Institute for Pharmacological Research, Milano; and
the Section of Pathology and Immunology, Department of Biotechnology,
University of Brescia, Brescia, Italy.
 |
ABSTRACT |
We have recently described a significant correlation between human
immunodeficiency virus-1 (HIV-1) RNA replication and monocyte chemotactic protein-1 (MCP-1) levels in the cerebrospinal fluid (CSF)
of individuals with the acquired immunodeficiency syndrome (AIDS) with
HIV encephalitis (E). Because local macrophages (microglia) are the
cells predominantly infected in the brain, we investigated whether in
vitro HIV infection affects MCP-1 production in mononuclear phagocytes
(MP). MCP-1 secretion and expression were consinstently upregulated
over constitutive levels in human monocyte-derived macrophages (MDM)
infected with the M-tropic R5 BaL strain of HIV-1. HIV replication was
required for this effect, as demonstrated by the absence of chemokine
upregulation after infection in the presence of
3'-azido-3'-deoxythimidine (AZT) or cell-exposure to heat-inactivated
( °) virus. MCP-1 induction was not restricted to HIV-1 BaL, but
was also observed during productive infection of MDM with two primary
isolates differing for entry coreceptor usage and of U937 cells with
the X4 HIV-1 MN strain. Based on the observation that exogenous HIV-1
Tat induced MCP-1 expression in astrocytes, we also investigated its
role in MDM and U937 cells. Exogenous Tat induced MCP-1 production from
MDM in a concentration-dependent manner, however, it was not effective
on uninfected U937 cells or on the chronically infected U937-derived
cell line U1. Transfection of Tat-expressing plasmids moderately
activated HIV expression in U1 cells, but failed to induce MCP-1
expression in this cell line or in uninfected U937 cells. HIV
replication-dependent expression of MCP-1 in MP may be of particular
relevance for the pathogenesis of HIV infection in nonlymphoid organs
such as the brain.
© 1999 by The American Society of Hematology.
| |
INTRODUCTION |
IN ADDITION TO CD4+ T
lymphocytes, mononuclear phagocytes (MP) have been earlier identified
as targets for human immunodeficiency virus (HIV) infection both in
vitro1,2 and in vivo.3,4 Because of the limited
HIV-induced cytopathic effects and their ability to accumulate high
levels of HIV particles in intracellular compartments,2,4-6
HIV-infected macrophages may serve as "Trojan horses" and
disseminate the virus in different organs, including the lungs, skin,
lymph nodes, and the brain (reviewed in Poli and Fauci7).
Of note, brain macrophages (microglia) are the main cells sustaining
HIV replication in this organ and represent the major cellular
determinant of HIV encephalitis (HIV-E), a pathological condition often
associated with dementia and other opportunistic
infections.3,4,8 Secretory products, including cytokines,
released by HIV-infected macrophages have been implicated in the
neuronal damage observed in acquired immunodeficiency syndrome (AIDS)
patients with dementia,9,10 although the mechanisms underlying monocyte recruitment to the brain are poorly understood. In
this regard, elevated levels of transforming growth factor- (TGF-), a cytokine with a potent chemotactic activity for
monocytes,11 have been described in brain tissue of AIDS
patients.12 In vitro, HIV infection upregulated production
of TGF- in monocyte-derived macrophages (MDM).12
Recently, in vitro HIV infection of MDM has been linked to increased
secretion of monocyte inflammatory protein-1 (MIP-1) and
MIP-1.13,14 Of note is the fact that MIP-1 mRNA was
detected in brain tissue of patients with HIV-E.13 These
findings suggest a potentially important contribution of these CC
chemokines in the recruitment of monocytes to the brain occurring in
some HIV-infected individuals.
Monocyte chemotactic protein-1 (MCP-1), a CC chemokine produced by MP,
is a potent activator of monocyte function.15,16 MCP-1
selectively binds to CCR2, a chemokine receptor shared with MCP-2, -3, and -4,15,16 although binding to CCR10 has also been
recently reported.17 MCP-1 has a crucial role in
monocyte recruitment in vivo in several organs and tissues, including
the brain, an observation supported by studies in transgenic mice overexpressing MCP-118-20 and in CCR2-deficient
mice.21-23 In addition, the role of MCP-1 in monocyte
infiltration in several inflammatory diseases has been
described.15,16
Regarding HIV infection, unlike MIP-1, MIP-1 and
regulated upon activation normal T-cell expressed and secreted
(RANTES), MCP-1 has not been previously associated with inhibition of
HIV infection,24 although CCR2 may act as coreceptor for
some HIV strains.25 However, inhibition of virus
replication by MCP-1 has been recently reported,26 and we
have observed modulation of virus replication by MCP-1 in ex vivo
cultures established from infected individuals.27 Of
interest, a selective accumulation of MCP-1, but not of other
chemokines, in the cerebrospinal fluid (CSF) of AIDS patients with
cytomegalovirus encephalitis (CMV-E)28 and, more recently,
also in patients with HIV-E29 and AIDS-associated dementia30 has been described, suggesting an important role of this chemokine in the pathogenesis of these HIV-associated diseases
of the central nervous system (CNS). In one of these studies,30 exogenous addition of Tat induced MCP-1
expression in cultures of human fetal brain astrocytes. Here we have
investigated whether HIV replication or cell stimulation by exogenously
added or endogenously expressed Tat could affect MCP-1 production in primary human MDM and in the U937 promonocytic cell line.
| |
MATERIALS AND METHODS |
MDM.
Monocytes were isolated from buffy coats of healthy HIV seronegative
blood donors by Ficoll-Hypaque and Percoll (Pharmacia, Uppsala, Sweden)
gradients, as described.31 Purity was  90%, as
determined by flow cytometry analysis for CD14 expression, using mouse
antihuman CD14 monoclonal antibody (MoAb) (IgG2a; Caltag Labs,
Burlingame, CA) followed by fluorescein isothiocyanate (FITC)-conjugated goat antimouse MoAb (Jackson Immunoresearch Labs,
Inc, West Grove, PA). Monocytes were seeded in 48-well plates (Falcon,
Becton-Dickinson Labware, Lincoln Park, NJ) at 0.2 × 106 cells/mL in Dulbecco's modified Eagle's medium (DMEM)
(BioWhittaker, Verviers, Belgium) supplemented with 10% fetal calf
serum (FCS) (Hyclone Europe, Oud-Beijerland, The Netherlands) and 5%
pooled HS. All media and sera were monitored for low content of
endotoxin by the lymulus amoebocyte lysate assay (BioWhittaker).
HIV infection of MDM.
Five to 7-day old MDM were infected with the M-tropic R5 BaL strain of
HIV-132 at the multiplicity of infection (MOI) of 0.1 or
with primary HIV isolates (4 × 103 cpm of reverse
transcriptase (RT) activity per 0.2 × 106 cells).
Fifty percent of culture media were replaced with fresh media twice a
week. Aliquots of culture supernatants were harvested at the indicated
time points and stored at  80°C. Primary HIV isolates were
established by cocultivation of HIV-infected patients' peripheral
blood mononuclear cells (PBMC) with phytohemagglutinin (PHA-P, 5 µg/mL, Sigma Chemical Corp, St Louis, MO) activated PBMC from
uninfected individuals. The fusogenic ability of the viruses was tested
on the standard human T-lymphotropic virus-1 (HTLV-1)-transformed MT-2
cell line, as previously described.33 Chemokine coreceptor
usage was tested on U87 astrocytic cells stably transfected with human
CD4 alone or together with one of the following human chemokine
receptors: CXCR4, CCR2B, CCR3, or CCR5, as reported.34
HIV infection of the promonocytic U937 cell line.
Promonocytic U937 cells35 were resuspended in RPMI 1640 (BioWhittaker), supplemented with 10% FCS (Hyclone Europe), at the concentration of 1 × 106 cells/mL and infected with
the X4 MN strain of HIV-1 (4 × 104 cpm RT activity
per 1 × 106 cells). After 1 hour of incubation, the
excess of free virus was removed by dilution with RPMI 1640 and
centrifugation; the cells were then seeded in duplicate cultures in
48-well plastic plates (Falcon, Becton Dickinson Labware) at the
concentration of 2 × 105 cells/mL/well. The cultures
were fed every 4 to 5 days with fresh medium. Aliquots of culture
supernatants were harvested and stored at 80°C.
U1 cell line.
The chronically HIV-infected U1 cell line was established by limiting
dilution cloning of U937 cells surviving the acute infection by
HIV-1LAI/IIIB.36 This cell line is
characterized by a constitutive state of relative latency and
inducibility by several cytokines and related agents.7,36
HIV-RT assay.
HIV replication, monitored as Mg++-dependent RT activity
released into supernatants, was measured as previously
described.37
Cytokine assays.
A homemade enzyme-linked immunosorbent assay (ELISA)28,29
was used to measure MCP-1 levels in culture supernatants, whereas a
commercially available ELISA kit for tumor necrosis factor (TNF)- was purchased from R&D Systems (Minneapolis, MN). Comparable
concentrations of MCP-1 were measured in parallel tests conducted with
this homemade and a commercially available ELISA kit (R&D Systems).
RT-polymerase chain reaction (PCR) detection of MCP-1 mRNA.
Total cellular RNA was isolated from MDM by RNAzol B (Duotech S.r.l.,
Milan, Italy) at different times after the beginning of the cultures in
the presence or absence of HIV. RNA (0.5 µg) was reverse transcribed,
and aliquots corresponding to 1/40 of the cDNA obtained were amplified
in a 50-µL volume of the reaction mixture in the presence of 1.25 U
AmpliTaq Gold DNA polymerase (Perkin-Elmer Corp, Norwalk, CT) and 1 µL antisense primer end-labeled with  -32P-adenosine
triphosphate (Amersham, Arlington Heights, IL), corresponding to
approximately 200,000 to 600,000 cpm. The housekeeping gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was amplified as
internal control. The sequences of the primers used and amplification conditions were previously reported.38 To test for the
linearity of amplification, twofold serial dilutions (seven dilutions
starting from 1:20) of a standard cDNA obtained by retrotranscribing 1 µg of total RNA extracted from PBMC isolated from a healthy donor and
stimulated for 6 hours with PHA39 were amplified in each PCR assay. The PCR products were analyzed by electrophoresis in 5%
polyacrylamide gels and visualized by autoradiography.
Experiments with HIV-1 Tat.
Lipopolysaccharide (LPS)-free (by the lymulus amoebocyte lysate assay)
full-length (1-86) synthetic Tat was purchased from Tecnogen (Piana di
Monte Verna, CS, Italy) and added at different concentrations to both
MDM and U937 or U1 cells, as further specified. Plasmids expressing
either Tat or Y26ATat, in which a tyrosine residue at position 26 was
replaced by alanine causing the loss of HIV-1 long terminal repeats
(LTR) transactivating capacity40 (kind gift of
Ben Berkhout, University of Amsterdam, Amsterdam, The Netherlands),
were transiently transfected into uninfected U937 cells or in
chronically infected U1 cells by diethyl aminoethyl (DEAE)
dextran.40
| |
RESULTS |
HIV infection superinduces MCP-1 secretion in human MDM.
MCP-1 was constitutively secreted by uninfected MDM, as previously
reported.41 However, a clear-cut upregulation of chemokine secretion was consistently observed in HIV-infected MDM
(Fig 1A), ranging from twofold to fivefold
increase over constitutive levels in seven individual experiments
performed with cells obtained from eight independent donors (Fig 1B).
Of interest, the peak of MCP-1 secretion paralleled the peak of virus
replication. TNF-, previously shown not to be induced by HIV
replication in MDM,13,42 was measured as a control, and it
was undetectable in our HIV-infected cultures (data not shown).
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| Fig 1.
HIV infection of MDM superinduces MCP-1 secretion. Human
MDM were infected with HIV-1 Bal (MOI: 0.1). Culture supernatants were
tested for MCP-1 and RT activity contents. (A) One experiment
representative of seven independently performed is shown. (B) MCP-1
levels measured at the peak of RT activity in seven independent
experiments with cells obtained from eight donors; the mean ± standard deviation (SD) is shown. ** P < .01 versus
uninfected by paired Student's t test. ( ) Uninfected; ( )
infected.
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HIV replication is required for MCP-1 induction in MDM.
Binding of HIV to CD4 has been reported to induce cytokine expression
in MDM.43,44 In other studies, viral replication was
required for cytokine induction.12-14 To rule out the
possibility that exposure to the virus could account for HIV-induced
MCP-1 secretion in our infected cultures, MDM were infected with HIV-1 BaL at the MOI of 0.1 in the presence or absence of 10 µmol/L 3'-azido-3'-deoxythymidine (AZT). In addition, MDM were exposed to
virus inactivated by heating at 56°C for 1 hour ( °-HIV).
Both AZT treatment and heat inactivation abolished virus replication and diminished MCP-1 secretion to the levels of uninfected MDM (Table 1). These findings support the
hypothesis that MCP-1 superinduction is dependent on virus replication.
HIV infection induces MCP-1 mRNA expression in human MDM.
To further explore MCP-1 regulation by HIV, we analyzed MCP-1
expression in MDM at different days postinfection and in parallel uninfected cultures by RT-PCR. In preliminary experiments, we observed
that MCP-1 mRNA was undetectable in freshly isolated monocytes, but was
induced at high levels after 20 hours of culture (data not shown), as
previously reported.41 High levels of MCP-1 expression were
found at the time of infection, after 5 to 7 days of culture (data not
shown), which remained elevated until days 10 to 12, before declining
(Fig 2). Higher levels of MCP-1 mRNA were
consinstently observed in HIV-infected MDM. Noteworthy, MCP-1 mRNA was
no longer detectable in uninfected MDM 15 days after infection, but it
was still clearly expressed in the parallel-infected cultures (Fig 2).
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| Fig 2.
Expression of MCP-1 mRNA in MDM after HIV infection. MDM
were infected with HIV-1 BaL (MOI: 0.1). Total RNA was extracted and
MCP-1 expression was measured by RT-PCR at the indicated days
postinfection. On normalization against GAPDH and given the arbitrary
value of 1 to the MCP-1 mRNA of uninfected cultures after densitometric
scanning (Molecular Dynamics, Sunnyvale, CA), RNA induction
levels in HIV-infected MDM were 1.4 at day 5 and 12.4 at day 10, respectively. The results are representative of three independent
experiments.
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MCP-1 secretion is upregulated in MDM after infection with two
primary isolates differing in coreceptor usage.
Two different primary HIV isolates (GRA and DUR, R5 monotropic and
X4/R5 dualtropic, consistent with their nonsyncytium inducing, NSI, and
SI phenotypes in MT-2 cells, respectively), were normalized for RT
activity counts (4 × 103 cpm/well/2 × 105 cells) and tested for MCP-1 induction in MDM. Both
viruses gave rise to a productive infection in MDM and superinduced
MCP-1 secretion (Fig 3).
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| Fig 3.
Primary HIV isolates (GRA and DUR) superinduce MCP-1
secretion in MDM. MCP-1 levels present in uninfected and infected
cultures at the peak of RT activity (day 28) are shown.
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HIV infection of U937 cells induces MCP-1 production.
U937 is a well-known promonocytic cell line35 that can be
productively infected with X4 strains of HIV-1,36,45
characterized by low constitutive secretion of MCP-1 inducible by
several agents, including phorbol esters, interleukin-6 (IL-6),
interferon- (IFN-), and TNF-.38 Therefore, we
tested whether HIV infection could modulate MCP-1 expression in this
cell line. MCP-1 was detected at very low levels in the supernatants of
uninfected cells, whereas HIV-1 MN-infected cells showed increased
MCP-1 secretion (Fig 4A). As observed with
MDM, the peak of MCP-1 production coincided with or slightly preceded
that of viral replication. In addition, the upregulation of MCP-1
secretion in HIV-infected cells was correlated to increased levels of
mRNA expression, as detected by RT-PCR (Fig 4B).
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| Fig 4.
HIV-1 MN infection of U937 promonocytic cells upregulates
MCP-1. (A) MCP-1 protein levels and RT activity were measured at the
indicated days postinfection. (B) MCP-1 expression measured by RT-PCR
in uninfected and HIV-infected U937 cell cultures from which chemokine
secretion was determined (A). RNA induction levels, calculated as
described in the legend to Fig 2, were 1.5 at day 10 and 4.7 at day 28 postinfection, respectively.
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Thus, upregulation of MCP-1 expression appears to be a general property
of replication-competent HIV, regardless of its ability to use
different chemokine receptors as ports of entry and/or its
T-lymphocytic versus macrophage in vitro cell tropisms.
Exogenous Tat stimulates MCP-1 secretion from MDM, but not from U937
or U1 cell lines.
In addition to its transactivating capacity consequent to binding to
the TAR RNA sequence of HIV,46,47 Tat has been shown to
modulate several cell functions, including cytokine
production.48,49 In particular, addition of exogenous Tat
to cultures of fetal astrocytes has resulted in the induction of MCP-1
expression.30 We, therefore, investigated whether a similar
mechanism was operational in our model systems. Of concern is the
possibility that LPS contamination may influence the results of these
experiments. For this reason, we tested our Tat preparation for the
presence of LPS contamination by the lymulus amoebocyte lysate assay,
and it was found to be negative. Both MDM from different donors and two
U937 cell lines, one sensitive (U937) and the other one (U1) known to
be insensitive50,51 to LPS stimulation, were incubated with
Tat at concentrations between 1 ng/mL and 1 µg/mL, and MCP-1 was
measured in the supernatants. Both cell lines secreted substantial
amounts of MCP-1 under stimulation by IL-6 or, in the case of U937
cells, by LPS, but they were totally unresponsive to exogenous Tat
(Fig 5). In contrast, MDM were induced to
secrete MCP-1 by Tat stimulation in a concentration-dependent manner
(Fig 5).
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| Fig 5.
Effect of exogenous Tat on MCP-1 secretion in U937 and U1
cell lines and in MDM. Both U937 and U1 cells (4 × 105
cells/mL) and 5-day old MDM of two donors were incubated with LPS (10 ng/mL), IL-6 (10 ng/mL), or Tat at the indicated concentrations. MCP-1
was measured in U937 and U1 culture supernatants after 48 hours and in
MDM culture supernatants after 72 hours of incubation.
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The potential role of endogenously expressed Tat was investigated by
transient transfection experiments in the U937/U1 cell systems. A
plasmid containing a functional mutation in tat (Y26ATat), known to
abolish its HIV transactivating activity,40 was used as a
control. Of note, endogenous Tat produced by U1 cells has been
characterized as nonfunctional.52 Transfection of
Tat-expressing plasmids, but not of control plasmids, resulted in a
modest, but clearly detectable, induction of HIV expression from U1
cells 96 hours after transfection (data not shown), consistent with previous reports.47,48,52,53 In contrast, no evidence of MCP-1 secretion was obtained either from U1 or uninfected U937 cells by
Tat transfection (data not shown).
Thus, Tat expression or secretion appears to be dispensable for
HIV-mediated induction of MCP-1 in monocytic cells.
| |
DISCUSSION |
In the present study, we have observed a superinduction of MCP-1
expression and secretion in MDM by productive HIV-1 infection. HIV-induced MCP-1 was not restricted to HIV-1 BaL, but was observed both in MDM infected with two primary isolates differing for entry coreceptor usage, and in U937 cells infected by the X4 laboratory adapted strain MN. Tat induced MCP-1 secretion in MDM, but not in the
U937 cell line and in chronically infected U937-derived U1 cells in
which activation of HIV expression by Tat was demonstrated.
The superimposable kinetics of MCP-1 secretion and virus replication in
HIV-infected MP together with the absence of MCP-1 superinduction after
infection in the presence of AZT or with °-HIV strongly indicate
a close linkage between HIV replication and MCP-1 induction. In this
regard, transcription of the human MCP-1 gene requires synergy between
two NF-kB/Rel dimers and Sp1, which is essential for the basal
transcription of this gene.54 A similar synergy between
NF-kB/Rel and Sp1 is crucial for HIV-1 gene expression.55
Of interest, several proinflammatory cytokines, including TNF-,
IL-1, and IL-6 have been reported to upregulate both HIV expression
(reviewed in Vicenzi et al56) and MCP-1 production.31,38,57 Recently, the HIV-1-encoded Tat gene
product has been shown to upregulate MCP-1 expression in
astrocytes.30 In consideration of the fact that Tat can
functionally interact with both NF-kB and Sp-1 cellular transcription
factors,58,59 this observation on the one hand supports the
hypothesis that MCP-1 and HIV expression could be transcriptionally
coregulated. On the other hand, our results indicate that Tat, either
endogenously expressed after transfection or exogenously added, is not
sufficient to induce MCP-1 secretion, at least in U937 cells, although
it stimulated production of this chemokine in MDM. The reasons for this
functional dichotomy are unclear, but they may be related to the
different stages of differentiation of these monocytic cells. In this
regard, Tat was shown to induce migration of monocytes by interaction
with the vascular endothelial growth factor receptor (VEGFR)-1/Flt-1 receptor.60 Of note, in
similar experiments, Tat failed to induce MCP-1 in moncytes (S.S. and
S.M., unpublished). In addition, VEGFR-1/Flt-1-dependent effects of
Tat were shown to peak sharply at 10 ng/mL and rapidly declining at
higher or lower concentrations,59 whereas Tat-dependent
induction of MCP-1 peaked at 100 ng/mL in MDM cultures established from
one donor and did not achieve plateau levels in those of a second
individual (Fig 5). The effects described here with exogenous Tat were
independent from detectable levels of LPS, as demonstrated by the fact
that this viral protein failed to induce MCP-1 production from
LPS-responsive U937 cells. Similar results were obtained when U937 and
U1 cells were transfected by a Tat-expressing plasmid. Although
activation of HIV expression was observed in U1 cells (but not in
control cultures transfected with a mutagenized Tat-expressing
vector40), this did not lead to MCP-1 expression. Similar
negative results were observed after parallel transfections of U937
cells (data not shown). The definition of the pathway involved in
Tat-mediated activation of MCP-1 in MDM, involving the dissection of
which domains of the viral protein are involved,61 deserves
further investigation.
At the clinical level, a correlation between plasma levels of MCP-1 and
HIV viremia has been recently reported in advanced AIDS
patients.62 A coregulation of MCP-1 expression and HIV replication would account for the significant and selective correlation existing between the elevated levels of HIV RNA and those of MCP-1 in
the CSF of AIDS patients with HIV-E, but not with other opportunistic diseases (with the exception of CMV-E) or without infections of the
CNS.28-30 Of note is the fact that HIV-E is a pathological condition mainly sustained by virus replication in brain macrophages (microglia) and astrocytes.3,4,8 Increased MCP-1 production by HIV replicating microglial cells may play an important role in the
recruitment of circulating monocytes to the brain, therefore feeding
the pathological inflammatory process sustaining HIV-E.
| |
ACKNOWLEDGMENT |
The authors thank Dr Ben Berkhout of the Department of Human
Retrovirology of the University of Amsterdam for provision of the Tat
expressing plasmids and Dr Chiara Bovolenta for helpful discussions.
| |
FOOTNOTES |
Submitted April 20, 1998; accepted October 28, 1998.
Supported by grants from the National Project for Research Against AIDS
of the Istituto Superiore di Sanità (ISS), Rome, Italy. M.M. is
the recipient of a fellowship from ANLAIDS, Rome, Italy. S.G. is a
fellow of ISS.
The publication costs of this
article were defrayed in part by
page charge payment. This article
must therefore be hereby marked
"advertisement"
in accordance with 18 U.S.C. section
1734 solely to indicate this fact.
Address reprint requests to Manuela Mengozzi, PhD, P2/P3
Laboratories, DIBIT, Via Olgettina n. 58, 20132 Milano, Italy;
e-mail: poli.guido{at}hsr.it.
| |
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ABSTRACT
INTRODUCTION