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Department of Immunology and Microbiology, Institute of Medical Biology, University of Southern Denmark, Odense, Denmark
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResults and DiscussionReferences |
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) of 71 residues
and an alternatively spliced form (M160-
) of 39 residues. M160-
contains three possible phosphorylation sites, which are lost in the
alternatively spliced form. RT-PCR analyses showed M160 to be expressed
by alveolar macrophages and by the monocyte cell lines HL60, U937, and
THP1, but not by Jurkat or Raji cells. Stimulation of U937 cells with
phorbol ester resulted in an increased expression of M160 from day 5
onward. RT-PCR analysis of 19 different human tissues showed signals
for M160- of varying intensity in all tissues, whereas M160- was
confined to the spleen. We conclude that M160 is a new member of the
scavenger receptor cysteine-rich superfamily expressed by the
monocyte/macrophage cell lineage. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResults and DiscussionReferences |
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The scavenger receptor superfamily was recognized during the analysis of the structure of the type I macrophage scavenger receptor (4, 5), a trimeric integral membrane protein found mainly on macrophages and involved in adhesion, host defense, and the pathogenesis of atherosclerosis (6, 7). As in other protein families such as the Ig family, the C-type lectin family and the epidermal growth factor family, the SRCR domains are found in secreted (8, 9, 10) and membrane-anchored proteins (11, 12) as single domains (4, 5), as part of multidomain mosaic proteins (1, 13), or as tandem repeats (3, 14, 15). Many SRCR domains are found on cells associated with the immune system (16), but SRCR domains are also synthesized by other cells, such as hepatocytes (9) and epithelial cells of the gastrointestinal tract (17, 18). Functionally, the SRCR domains are thought to mediate protein-protein interactions and ligand binding (6, 7).
The domain that defines the SRCR family of proteins consists of
100–110 amino acid residues (16). Molecules with SRCR
domains are divided into two groups based on the localization and
number of cysteine residues. Members of group A all have six cysteine
residues and lack cysteine residues at positions 1 and 4. Members of
group B have either eight or six cysteine residues, but the cysteine
residues at positions 1 and 4 are always present (16).
Another difference between group A and B SRCR proteins is seen at the
genomic level, where group A SRCR domains are encoded by two different
exons, whereas group B SRCR domains are encoded by a single exon. The
structure of the group A SRCR domain from Mac-2 binding protein has
recently been determined by x-ray crystallography (19).
This revealed a compact fold consisting of a curved 6-stranded
-sheet cradling an helix, and structure-based sequence alignment
showed that this structure could be used as a template for the entire
SRCR superfamily (19). Group B SRCR domains have so far
only been found in vertebrates, whereas group A SRCR domains have been
found in phyla ranging from vertebrates to the most primitive
metazoa.
On the basis of their structure, sequence homologies, and domain
organization, members of the group B SRCR family can be divided into
three subgroups. The most extensively studied subgroup comprises CD5
(11), CD6 (12), and SP (10).
CD5 and CD6 have an extracellular region composed of three SRCR
domains, a transmembrane domain, and a cytoplasmic region. SP has
three SRCR domains, showing high homology with CD5 and CD6, but lacks
the transmembrane and cytoplasmic domains (10). CD5 and
CD6 are predominantly expressed by thymocytes, mature T cells, and a
subset of B cells involved in the regulation of T cell activation.
Tyrosine residues in the cytoplasmic region of CD5 are transiently
phosphorylated after activation of the T cells (20, 21, 22),
and T cells in CD5-deficient mice are hyperresponsive to stimulation
(23, 24), indicating that CD5 may act as a negative
regulator of TCR-mediated signal transduction (23).
Although CD5 and CD6 are closely related structurally, their ligands
show no homology. CD5 has been shown to bind CD72 (25),
and other candidate CD5 ligands have been described that are all
compatible with a role in T cell/B cell interaction
(26, 27, 28). CD6 binds to the activated leukocyte cell
adhesion molecule ALCAM (29), the binding being mediated
by the membrane-proximal SRCR domain of CD6 and the
amino-terminal Ig domain of ALCAM (30). Transcripts
encoding Sp are found in human bone marrow, spleen, lymph nodes,
thymus, and fetal liver, but not in nonlymphoid tissues. Sp binds
specifically to peripheral monocytes but not to T or B cells
(10).
The second subgroup within the SRCR group B molecules includes gp-340 (1), DMBT1 (31), and their murine and rabbit counterparts CRP-Ductin (18), Ebnerin (17), and Hensin (32). Bovine gall-bladder mucin (33) and Pema SREG from the sea lamprey Petromyzon marinus (34) are also related to this subgroup. These molecules are synthesized by epithelial cells in the gastrointestinal tract and in ducts of exocrine glands. Gp-340 binds specifically to SP-D and is also synthesized by macrophages. Hensin is found in the proximal tubules of the kidney and has been suggested to induce the reversal of polarity of the intercalated cell, i.e., to shift the anion exchanger from the apical to the basolateral cell membrane (17).
The third subgroup of SRCR group B molecules is the WC1 family, comprising WC1 and CD163 (3). The WC1 gene is expressed by T cells of the cow (14), sheep (35), and pig (36). Bovine WC1 is composed of 11 SRCR domains, a transmembrane region, and a cytoplasmic domain (14). So far, four different forms of WC1 have been identified in pigs, representing both alternative spliced forms of the same gene and products of different genes (36). The largest of the pig WC1 genes encodes five SRCR domains. CD163 was originally defined by five different mAbs as a human monocyte/macrophage-associated Ag found on all circulating monocytes and on most tissue macrophages (37). Cloning of CD163 revealed that this protein is a membrane protein composed of nine type B SRCR domains followed by a transmembrane region and a cytoplasmic domain. No function has so far been described for the WC1 family of proteins.
We here report the primary structure of a new member of the WC1 family, which we have named M160 and characterized as a molecule primarily related to the monocyte/macrophage cell lineage.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResults and DiscussionReferences |
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Media and supplements were purchased from Life Technologies (Grand Island, NY). HL60, U937, Jurkat, and Raji cells were cultured in RPMI 1640 medium supplemented with 10% heat inactivated FCS, 2 mM L-glutamine, 100 IU/ml penicillin, and 100 µg/ml streptomycin. THP1 cells were grown in the same medium containing 0.05 mM 2-ME (M 7522; Sigma, St. Louis, MO). Cell viability was assessed by erythrosin B exclusion.
U937 cells in the logarithmic growth phase were incubated at 2 x 105 cells/ml for up to 9 days in the presence of 100 ng/ml PMA (Sigma P8139). The cells were removed from the culture flask with a rubber policeman and washed in PBS containing 0.1% human serum albumin (HSA). Peripheral blood was lysed by the ammonium chloride method, and peripheral blood leukocytes were washed three times in PBS. Bronchoalveolar washings were provided by Odense University Hospital, and cells from these were isolated by centrifugation and washed three times in PBS.
cDNA cloning and sequencing
A previously isolated cDNA clone (gp-clone 7) spanning residues 3691–5499 of gp-340 cDNA was labeled with 32P and used to screen a human oligo(dT)-primed lung cDNA library (Stratagene no. 93210). Gp-clone 7 covers four and one-half SRCR domains, four SRCR-interspersed domains (SIDs), and one-half CUB domain (a domain first found in complement component C1r/C1s, Uegf, a sea urchin epidermal growth factor-containing protein, and Bmp1, bone morphogenetic protein 1). Approximately 2.4 x 105 individual clones were screened. Positive clones were replated, rescreened, subcloned, and sequenced.
Sequence analysis revealed that one clone (Z-2) included an SRCR sequence that was different from the SRCR sequences found in gp-340. Part of the sequence of clone Z-2 was identical with an expressed sequence taq clone (za25d06). This clone was obtained and sequenced. Clone Z-2 was used as probe to screen >5 x 106 individual clones from three different libraries. The libraries were a human lung 5'-stretch plus cDNA library (HL3004b; Clontech Laboratories, Palo Alto, CA), a human lung cDNA library in the Uni ZAP-XR vector (937210; Stratagene, La Jolla, CA), and a human alveolar macrophage cDNA library in the Lambda Zap Express vector (Stratagene), prepared as follows. Briefly, RNA was purified from bronchoalveolar lavage cells from 14 different individuals by means of the RNeasy Midi kit (Qiagen, Chatsworth, CA). Eighty micrograms of total RNA was obtained and used for the purification of messenger RNA using the Oligotex mRNA Mini kit (Qiagen). The yield of mRNA was 1.2 µg. This mRNA was then used to synthesize a cDNA library in strict accordance with the manufacturer’s protocols (Stratagene Lambda Zap Express cDNA synthesis kit and Lambda Zap Express Gigapack III gold cloning kit). No positive clones were obtained on screening these three cDNA libraries; therefore, another strategy was adopted.
By aligning the individual SRCR domains of M130 and the three known
SRCR domains of Clone Z-2, two degenerated forward primers were
designed (Deg forw SRCR1 9-26 and Deg forw SRCR1 125-148; Table I
). These two degenerated primers were
used as sense primers in all of the subsequent RT-PCR procedures. For
each round of RT-PCR, a set of three M160-specific antisense primers
was designed, one for first-strand cDNA synthesis (SP1), another for
nested PCR (SP2), and a third for sequencing (SP3). Total RNA (2 µg)
isolated from human spleen (Clontech) was used for first-strand
synthesis using the antisense primers SP1 (a, b, c, d, and e).
First-strand cDNA synthesis was performed with avian myeloblastosis
virus reverse transcriptase supplied with the 5'/3'-rapid amplification
of cDNA end (RACE) kit (Boehringer Mannheim, Indianapolis, IN) at
55°C according to the manufacturer’s protocol. The resulting
single-stranded cDNA was purified with the High Pure PCR Product
Purification kit (Boehringer Mannheim) and subjected to nested PCR. The
reaction was performed in a final volume of 30 µl 50 mM Tris-HCl, pH
9.2, containing 16 mM
(NH4)2SO4
and 2 mM MgCl2, with 3 µl cDNA, 25 pmol of each
of the primers, 200 µM of each dNTP (Amersham Pharmacia Biotech,
Piscataway, NJ), and 1 U Taq DNA polymerase (Amersham
Pharmacia Biotech). After an initial denaturation for 2 min at 94°C,
40 cycles of 94°C for 30 s, 53°C for 30 s, 72°C for 2
min, and 72°C for 7 min were conducted with the specific primers SP2
(a, b, c, d, and e) in combination with Deg forw SRCR1 9-26 or Deg forw
SRCR1 125-148. The resulting products were isolated by preparative
agarose gel electrophoresis, purified with Sephaglas BrandPrep kit
(Amersham Pharmacia Biotech) and sequenced using the SP3 (a, b, c, d,
and e) primers in the DNA sequence reactions. A total of five rounds of
"degenerated" RT-PCR were performed.
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To reach the 5' untranslated region, a last set of specific primers (SP1f, SP2f, and SP3f) were designed. The 5'-RACE reaction was performed with the 5'/3'-RACE kit (Boehringer Mannheim). First-strand synthesis was performed using 2 µg total RNA from the spleen as template and SP1f as primer. The resulting single-stranded cDNA was purified with the High Pure PCR Product Purification kit (Boehringer Mannheim) and poly(A) was added by means of the terminal transferase supplied with the kit. PCR was performed with the poly(T) primer and SP2f. The 5'-RACE products were then purified and sequenced.
Long-range PCR
From the sequences obtained from the 5' and 3' untranslated regions, sense (5' primer) and antisense (3' primer) primers were designed and used for long-range PCR to obtain full-length cDNA clones.
Poly(A)-RNA isolated from human spleen total mRNA (Clontech) was purified by means of the RNeasy Mini kit (Qiagen) and transcribed into cDNA by means of the Lambda ZAP Express Synthesis kit (Stratagene). Long-range PCR was conducted in a final volume of 30 µl by means of the Takara LA PCR kit (Biotechline, Copenhagen, Denmark). cDNA (0.5 µl) corresponding to 1 µg of cDNA was used as template, and 25 pmol of each primer (5' primer, 3' primer) were added. After denaturation for 2 min at 95°C, 30 cycles of 95°C for 30 s, 55°C for 45 s, and 68°C for 10 min were followed by a final extension step of 68°C for 15 min. The product was isolated by preparative agarose gel electrophoresis and purified with the Sephaglas BrandPrep kit (Amersham Pharmacia Biotech). Purified PCR products were ligated into the PCRIIvector and transformed into INVaF' One Shot using the Original TA cloning kit (Invitrogen). Plasmids from four clones were purified by means of the Quantum Prep Plasmid Miniprep kit (Bio-Rad, Richmond, CA) and sequenced in both directions.
Sequence analysis
The DNA sequence reactions were performed with the Prism Ready Reaction BigDyeDeoxy Terminator sequencing kit (PE Applied Biosystems, Allerød, Denmark). Samples were subjected to electrophoresis on an ABI prism 310 Genetic Analyzer, read automatically, and recorded using ABI Prism Model Version 2.1.1. software (PE Applied Biosystems).
Northern blot analysis
A tissue Northern blot was purchased from Clontech (no. PT1200-1)
and hybridized in 5 ml ExpressHyb solution at 68°C according to the
manufacturer’s instructions. The hybridization probe was a PCR
fragment spanning base pairs 4080–4493 from the 3' end of M160 cDNA.
One hundred microliters of the PCR fragment was radiolabeled with
[32P]dCTP (Amersham Pharmacia Biotech) by means
of an oligolabeling kit (Amersham Pharmacia Biotech). The Northern blot
was normalized with a -actin probe supplied by the manufacturer. The
blot was washed under high stringency conditions according to the
protocol and used to expose x-ray film (BioMax MS; Kodak, Rochester,
NY) with a double screen for 1 wk for the M160 probe and overnight
without screen for the -actin probe.
RT-PCR analysis
Samples of total RNA isolated from various human tissues were
obtained from Clontech. Samples of total RNA from 
2–5 x
106 cells of the cell lines HL60, U937, THP1,
Raji, and Jurkat, and from alveolar macrophages, were purified by means
of the RNeasy mini kit (Qiagen). RT-PCR was performed as duplex RT-PCR
using -actin as a standard. Total RNA was used for first-strand
synthesis and primed by the two primers RT-PCR actin rev1 and RT-PCR
M160 rev1. The reaction was conducted according to the protocol for
SuperScript II (Life Technologies) in a volume of 19 µl with 1.5 µg
of total RNA, 2 pmol of each primer, 4 µl of 5x first-strand buffer,
10 mM DTT, and 0.2 mM dNTP. The mixture was heated to 70°C for 10 min
and then cooled to 42°C when 1 µl (200 U) SuperScript II (Life
Technologies) was added. The mixture was incubated for 1 h at
42°C and finally heated to 70°C for 15 min.
Duplex PCR was performed in two rounds. A first round of 10 cycles using only the M160 specific primer RT-PCR M160 rev2 and RT-PCR M160 forw was conducted in 30 µl 50 mM Tris-HCl, pH 9.3, containing 16 mM (NH4)2SO4 and 2 mM MgCl2, with 3 µl of the first strand mixture, 25 pmol of each primer, 200 µM dNTP, and 1 U of Taq polymerase (Amersham Pharmacia Biotech). Cycling parameters were 94°C for 2 min followed by 10 cycles of 94°C for 30 s, 53°C for 30 s, and 72°C for 45 s. The second round of 20 cycles was run with primers specific for both actin and M160. The PCR was conducted in 30 µl 50 mM Tris-HCl, pH 9.3, containing 16 mM (NH4)2SO4 and 2 mM MgCl2, with 5 µl of the product from the first round as template, 25 pmol of each primer, 200 µM dNTP, and 1 U of Taq polymerase (Amersham Pharmacia Biotech). After an initial denaturation for 2 min at 94°C, 20 cycles of 94°C for 30 s, 53°C for 30 s, and 72°C for 45 s were performed. Ten microliters of each PCR product was run on a 2% agarose gel. To confirm the identity of the band obtained, bands of the relevant size were purified and sequenced.
Likewise, RT-PCR was performed with four different sets of primers
specific for CD163, actin, TNF-, and M160, respectively, on mRNA
from U937 cells harvested on day 0 (before PMA stimulation) and on days
1, 3, 5, 7, and 9 after stimulation with PMA. RNA from the cells was
purified by means of the RNeasy Mini kit (Qiagen). First-strand
synthesis was performed as described for tissue RNA, but with a mixture
of four different first-strand primers (RT-PCR TNF- rev 1, RT-PCR
actin rev1, RT-PCR CD163 rev1, and RT-PCR M160 rev1). PCR was performed
in four different reactions with 2 µl of the first-strand reaction
product as template and using 18 cycles for the actin reaction, 23
cycles for the M160 reaction, and 28 cycles for the TNF- and CD163
reactions. The resulting products were analyzed on 2% agarose gels.
The primers used were as follows: for actin, RT-PCR actin forw and
RT-PCR actin rev2; for CD163, RT-PCR CD163 forw and RT-PCR CD163 rev2;
for TNF-, RT-PCR TNF- forw and RT-PCR TNF- rev2; and for M160,
RT-PCR M160 forw and RT-PCR M160 rev2.
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Results and Discussion |
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TopAbstractIntroductionMaterials and MethodsResults and DiscussionReferences |
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A). No SIDs were found
between the SRCR domains, and although the repeated SRCR domains of
gp-340 showed a high degree of domain-to-domain homology (88–100%
identity at the protein level), the complete SRCR domains of the new
polypeptide showed only 29% identity between themselves and an average
identity with gp-340 SRCR domains of 32 and 56%, respectively. A
database search showed a high degree of homology, but not identity,
with human CD163 (M130) and bovine WC1, and the molecule was
provisionally designated M160. No untranslated 3' end or 5' ends were
found. By database screening, a human expressed sequence taq clone was
identified (za25d06) that showed 100% identity with the 5' end of
clone Z-2 and that also included a 3' end and a poly(A) tail.
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900 bp each, covering approximately three SRCR domains (Fig. 1
A). The fifth round gave a product of 350 bp covering one
SRCR domain, and the sixth round gave no product. Subsequently, 5'-RACE
PCR was performed on spleen RNA using specific sense primers and
poly(T) primers. This reaction generated a 350-bp product. The sequence
of this product showed homology with the sequence encoding the signal
peptide of CD163 (Fig. 1B). The translated sequence included
a putative leader sequence of 42 aa followed by a sequence that
showed high homology with the experimentally determined N-terminal
sequence of CD163 (Fig. 1B) (3).
Primers from the 5' and 3' untranslated ends were designed and used for
long-range PCR with RNA purified from alveolar macrophages as template.
A 4545-bp cDNA was obtained, subcloned, and sequenced in both
directions. The open reading frame encodes a polypeptide of 1453 aa,
including a possible hydrophobic signal sequence of 42 aa. The complete
nucleotide sequence of M160 has been deposited at the GeneBank
nucleotide sequence data base (accession no. AF264014) (Fig. 2).
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). All of the SRCR domains except SRCR 11 contain eight cysteine
residues and belong to group B of the SRCR family. SRCR 11 is an
atypical group B SRCR domain in that it lacks the Cys 2-Cys 7 bridge. A
model of SRCR 11 of M160 based on the crystal structure of Mac-2
binding protein analyzed with the SwissPdbViewer suggests that the
replacement of Cys 2 and Cys 7 by Gly and Ser, respectively, in SRCR 11
does not change the overall conformation of the domain (data not
shown). An alignment of the SRCR domains of M160 compared with the SRCR
domains of CD163 and WC1 in the cow and pig is shown in Fig. 3. SRCR 8 of CD163 and SRCR 1 in both
bovine and porcine WC1 and the second SRCR domain of CD5 also lack
the Cys 2-Cys 7 bridge.
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). In these domains an extra Cys
(Cys 6') residue is found between Cys 6 and Cys 7. In all three domains
Cys 6' is flanked by proline residues and the 3' proline is followed by
two Gly residues. This sequence allows for a turn, and it is possible
that Cys 6'-Cys 7 form a bridge stabilizing loop E-F. The sequence contains 17 potential N-glycosylation sites, the first of which is located at the predicted position -1 and is therefore probably not used. A conserved glycosylation site is found in loop E-F between the Cys 5-Cys 6 disulfide bridge in six of the M160 SRCR domains, and the same glycosylation site is found in CD163 in five of nine SRCR domains. This glycosylation site is not found in any of the sixteen known WC1 SRCR domains and is therefore specific for the SRCR domains found on macrophages and may be related to macrophage function.
The homologies between the SRCR domains of M160 vary from 18 to 61%
identity, domain 11 being the least well conserved. A long-range repeat
of SRCR domains has previously been identified in bovine WC1 and in
CD163 (3, 14) (Fig. 4).
Multiple alignments and sequence homologies revealed that M160 has a
similar repeating structure. This long-range repeating structure is
composed of five consecutive SRCR domains with a small 31 amino acid
residue linking domain between the second and third SRCR domains. This
cassette has been designated a [b-c-d-e-d] cassette, where the WC1
domains 1–11 are arranged as a-[b-c-d-e-d] [b-c-d-e-d] and the
CD163 domains are arranged as h-i-j-k-[b-c-d-e-d] (16).
The M160 SRCR domains 7–12 can similarly be arranged as
k-[b-c-d-e-d] with up to 75 and 77% identity between the SRCR
domains of the M160 cassette and those of CD163 and WC1 cassettes,
respectively. The "d" domains are the most highly conserved domains
within and between the cassettes. The first six domains of M160 show
identities between 40 and 61%, and these domains are similar to the
h-i-j domains in CD163, with an overall identity of 52–57%. It is
difficult to determine a precise hierarchy of relationships between
these domains, but it is possible that CD163 emerged by a gene
duplication of M160 and that three of the first six SRCR domains of
M160 were lost in this process. The recent assignment of the gene
encoding M160 to chromosome 12q13.3, close to the CD163 gene, supports
this notion (38).
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26 aa residues, and a cytoplasmic domain of
71 residues.
Northern blot analysis using M160 cDNA as probe revealed that mRNA
encoding M160 is expressed in the spleen, lymph nodes, thymus, and
fetal liver, whereas only weak expression was found in bone marrow and
no expression was found in peripheral blood leukocytes (Fig. 5). The tissues expressing mRNA encoding
M160 expressed only one transcript of 4.7 kb. The difference of only 96
bp between the M160- and the M160- variant forms described below
is probably below the resolution limit of the Northern blot
analysis.
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A). When spleen mRNA was used
as template, two clear bands were revealed (Fig. 6A). The
sequences of these two bands showed that the cytoplasmic domain of M160
occurs as two variant forms (Fig. 7), a
predominant form (M160-) of 213 nt, and an alternatively spliced
form (M160-) that lacks an in frame insertion of 96 nucleotides.
Thus M160- and M160- have cytoplasmic domains of 71 and 39 aa
residues, respectively. In this context it is interesting to note that
two polyadenylation sites are found in the 3' untranslated end of M160
cDNA. M160- includes the consensus sequence for protein kinase C
(R-[X]2-S/T-RR) (39), casein kinase II (S/T [X]2-D/E)
(40), and cGMP-dependent kinase (R/K-R/K-X-S/T)
(41), and these possible phosphorylation sites are all
absent in M160-. This suggests that M160- may be involved in
signal transduction through phosphorylation of the cytoplasmic domain
and the relative expression level of the M160- and M160- forms
may be involved in regulating this signal transduction.
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Different cell lines were then analyzed for the presence of M160 mRNA.
RT-PCR analysis showed M160 mRNA expression in THP1 and U937 cell lines
and low-level expression in HL60 cells and alveolar macrophages, but no
expression in Jurkat or Raji cells (Fig. 6B).
PMA stimulation of U937 cells provoked a small, delayed increase in
M160 mRNA expression from day 5. In the same cells, transcripts of
TNF- appeared on day 0 and peaked on day 3 (Fig. 6C). In
contrast to M160, no expression of CD163 mRNA was found in resting U937
cells (Fig. 6C), but PMA stimulation led to an increase in
CD163 mRNA on day 3. These results indicate that the constitutive
expression of CD163 and M160 differs and that these structurally
closely related molecules are differentially regulated.
We conclude from the above results that M160 is a multidomain protein composed of twelve SRCR domains, a transmembrane region, and a cytoplasmic domain. The cytoplasmic domain is found in two alternatively spliced forms, one of which contains three potential phosphorylation sites. Therefore, it is possible that signaling through M160 could be regulated via alternative splicing of cytoplasmatic encoding exons. Our data suggest that M160 expression, like that of CD163, is restricted to the monocyte/macrophage lineage, and that its expression may be increased by stimulation with phorbol ester.
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Footnotes |
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2 Address correspondence and reprint requests to Dr. Uffe Holmskov, Immunology and Microbiology, Institute of Medical Biology, University of Odense, Winslowparken 21.1, DK-5000 Odense C, Denmark.
3 Abbreviations used in this paper: SP-D, lung surfactant protein D; SRCR, scavenger receptor cysteine-rich; SID, SRCR-interspersed domain; RACE, rapid amplification of cDNA end.
Received for publication July 24, 2000. Accepted for publication September 7, 2000.
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References |
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TopAbstractIntroductionMaterials and MethodsResults and DiscussionReferences |
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  J. G. Calvert, D. E. Slade, S. L. Shields, R. Jolie, R. M. Mannan, R. G. Ankenbauer, and S.-K. W. Welch CD163 Expression Confers Susceptibility to Porcine Reproductive and Respiratory Syndrome Viruses J. Virol., July 15, 2007; 81(14): 7371 - 7379. [Abstract] [Full Text] [PDF]
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