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Journal of Bacteriology, January 2000, p. 508-512, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
The C-Terminal Portion of the Tail Fiber Protein of
Bacteriophage Lambda Is Responsible for Binding to LamB, Its Receptor
at the Surface of Escherichia coli K-12
Jiang
Wang,1
Maurice
Hofnung,1,* and
Alain
Charbit2,*
Unité de Programmation
Moléculaire et Toxicologie Génétique, CNRS URA1444,
Institut Pasteur, 75724 Paris Cedex 15,1 and
Unité INSERM U411, Faculté de Médecine
Necker-Enfants Malades, 75730 Paris Cedex 15,2
France
Received 6 August 1999/Accepted 12 October 1999
 |
ABSTRACT |
Bacteriophage 
adsorbs to its Escherichia coli K-12
host by interacting with LamB, its cell-surface receptor. We fused
C-terminal portions of J, the tail fiber protein of , to
maltose-binding protein. Solid-phase binding assays demonstrated that a
purified fusion protein comprising only the last 249 residues of J
could bind to LamB trimers and inhibited recognition by anti-LamB
antibodies. Electron microscopy further demonstrated that the fusion
protein could also bind to LamB at the surface of intact cells. This
interaction prevented adsorption but affected only partially
maltose uptake.
| |
TEXT |
Bacteriophage adsorbs to the
surface of Escherichia coli K-12 by interacting with the
outer membrane protein LamB (10). LamB is a trimeric protein
that forms nonspecific channels through the outer membrane
(11), allowing the diffusion of small hydrophilic molecules
(<600 Da). In addition, LamB is a sugar-specific porin that
facilitates the diffusion of maltose and maltodextrins into the cell.
Genetic analyses of LamB mutants tightly blocking phage adsorption
allowed the identification of a series of amino acid sites, clustered
mainly on three cell surface-exposed loops of the protein (reviewed in
references 2 and 4). Genetic analyses of mutants of able to use
such mutated LamB receptors (7, 14) showed that the amino
acid substitutions responsible for this compensatory or suppressor
effect were all located in the C-terminal portion of J, a
1,132-amino-acid protein constituting the tail fiber of . This
suggested strongly that the C-terminal portion of J was interacting
with LamB, but did not exclude totally that suppression could be due to
a long-range effect and that another part of J, such as the N-terminal
portion, was responsible for direct interaction with LamB.
In the present work, we directly tested the capacity of the C-terminal
portion of J fused to maltose-binding protein (MBP) to bind to LamB.
Genetic coupling to MBP allowed the purification of the fusion proteins
by affinity chromatography with an amylose column under nondenaturing
conditions, and the MBP moiety was used as a tag to reveal the fraction
of MBP-J bound to LamB. We were able to demonstrate for the first time
that the 20% distal portion of J was sufficient to allow binding to
the LamB receptor in vitro and in vivo.
Construction, expression, and purification of the MBP-J hybrid
proteins.
Genetic constructs which expressed three fusion proteins
consisting of the distal portion of the J protein of fused to the C-terminal end of the carrier MBP were made. The shortest fusion protein, designated MBP-J/S, contained residues 884 to 1132 of J (i.e.,
249 residues). The two larger MBP-J fusion proteins, designated MBP-J/M
and MBP-J/L, contained 100 and 200 additional residues of J, respectively.
Purified DNA from gene J of phage h+ (laboratory
collection), coding for the wild-type J protein, was used as the
template DNA in PCR performed to produce the 3' end of the J
gene. Three pairs of primers were used to generate the three
double-stranded DNA fragments flanked by EcoRI and
HindIII sites. The oligonucleotides of the 5' ends
(coding strands) were 5'-CG GAA TTC ATG GAG GAC ACG GAG GAA
GGC-3', 5'-CG GAA TTC GAT TAT TAC TTT TAT ATC CGC-3', and
5'-CG GAA TTC GCG CTG GGG AAC TAC AGG CTG-3' (the
EcoRI site is underlined). The oligonucleotide of the 3' end
of J (complementary strand) in all three cases was as
follows: 5'-CC AAG CTT TCA GAC CAC GCT GAT GCC CAG-3' (the
HindIII site is underlined). Oligonucleotides were
synthesized by Genset (Paris, France).
The pMAL-c vector (New England Biolabs, Beverly, Mass.) used to
construct the three C-terminal MBP-J fusion proteins carries
a deletion
of the signal sequence of MBP and therefore directs
the expression
(under the control of the
isopropyl-
-
D-thiogalactopyranoside
[IPTG]-inducible
ptac promoter) of the fusion proteins in the
cytoplasm of
the host cells. The PCR fragments were inserted downstream
of the
malE gene (between the
EcoRI and
HindIII sites). The LamB-negative
mutant of
E. coli K-12, JM 501 (
14), was the recipient for the
recombinant plasmids. The amounts of MBP-J fusion proteins MBP-J/L,
MBP-J/M, and MBP-J/S expressed under IPTG-induced conditions
corresponded
to 17, 23, and 32%, respectively, of whole-cell proteins
(data
not shown). MBP-J/M and MBP-J/S were chosen for further
purification.
IPTG-induced cultures were broken by passage through a
French
press, and the MBP-J hybrid proteins were purified by affinity
chromatography with an amylose column as previously described
(
12). Densitometric scanning of Coomassie blue-stained gels
(Fig.
1) indicated that MBP-J/M and
MBP-J/S were more than 90%
pure. In both constructs, no major
proteolytic cleavage products
were detected by Western blot with
anti-MBP serum (data not shown).
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FIG. 1.
Sodium dodecyl sulfate-10% polyacrylamide gel
electrophoresis of the purified proteins. From left to right, the sets
of lanes contain MBP-J/M (residues 784 to 1132 of J), MBP-J/S (residues
884 to 1132 of J) (for the two hybrid proteins, amounts were as
follows: lanes 1, 15 µg; lanes 2, 10 µg; and lanes 3, 5 µg), and
purified MBP (loaded as a control [lanes 1, 2, and 3 contain 30, 20, and 10 µg of protein, respectively]). The gel was stained with
Coomassie brilliant blue R-250.
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Interaction with purified LamB trimers in vitro.
Three
different solid-phase binding assays (Western blot, dot blot, and
enzyme-linked immunosorbent assay [ELISA]) demonstrated that the
distal portion of the tail fiber protein J of was sufficient to allow binding to LamB trimers in vitro.
Dot blot and Western blot.
In the dot blot and the Western
blot assays (Fig. 2), performed
essentially as described in reference 13, the two
hybrid proteins MBP-J/M and MBP-J/S yielded similar results. Only the data obtained with MBP-J/S are presented and discussed below. Nitrocellulose strips were coated with decreasing amounts of native purified LamB protein, wild-type MBP (MBPwt), or bovine serum albumin
(BSA), and the nitrocellulose strips were incubated with purified MBP-J
protein. As shown in Fig. 2A, the anti-MBP serum (a polyclonal antibody
against purified MBP raised in rabbits [9]) reacted
strongly with the spots corresponding to LamB and to MBPwt on the sheet
preincubated with MBP-J but only with the spots corresponding to MBPwt
on the nonpreincubated sheet. There was no nonspecific binding of BSA
or MBPwt to LamB, and the anti-MBP serum did not cross-react
nonspecifically with LamB or BSA. The Western blot assay further
indicated that the MBP-J hybrid protein bound to LamB trimers but not
to the denatured LamB monomers (Fig. 2B). This result does not rule out
the idea that the hybrid protein would bind to native LamB monomers,
although, to our knowledge, the existence of such a species has not
been demonstrated.
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FIG. 2.
Binding to LamB used to coat nitrocellulose. (A) Dot
blot binding assay. Nitrocellulose was coated with decreasing amounts
of either purified LamB trimers (lanes 1, 1 µg; lanes 2, 0.5 µg;
lanes 3, 0.1 µg; and lanes 4, 0.05 µg), purified MBPwt (lanes 1, 20 µg; lanes 2, 10 µg; lanes 3, 5 µg; and lanes 4, 1 µg) or BSA
(lanes 1, 10 µg; lanes 2, 5 µg; lanes 3, 1 µg; and lanes 4, 0.5 µg). After saturation with 2% gelatine, the sheet on the left part
of the figure was preincubated with MBP-J/S at a final concentration of
5 µg/ml. The control sheet on the right part of the figure was not
preincubated. (B) Western blot binding assay. Sodium dodecyl
sulfate-10% gels were loaded with decreasing amounts of purified LamB
trimers (from 4 to 0.5 µg as indicated on the figure). Samples were
either resuspended in native loading buffer (without
-mercaptoethanol) and incubated at 37°C for 10 min (lanes N) or
resuspended in denaturing loading buffer (with -mercaptoethanol) and
incubated at 100°C for 10 min (lanes d). The proteins were
transferred electrophoretically onto nitrocellulose. After saturation,
the sheet was preincubated with MBP-J/S (5 µg/ml). The unbound MBP-J
hybrid was eliminated by extensive washes in PBS-0.1% Tween 20. We
also performed the assay with a control sheet coated with the same
samples but not preincubated with MBP-J hybrid. In the absence of
preincubation, nothing was detected (data not shown). Lane MW,
molecular weight markers. LamB T., LamB trimers.
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ELISA.
The ability of the short MBP-J fusion protein (MBP-J/S)
to bind to purified LamB trimers was quantified in an ELISA.
Microtitration plates (Nunc-Immuno; Inter Med, Roskilde, Denmark) were
coated with a suspension of LamB trimers at a concentration of 1.5 µg/ml (100 µl per well) and incubated overnight at 37°C. The
plates were washed and then saturated with 2% gelatine for 2 h at
37°C. After several washes in phosphate-buffered saline (PBS), serial dilutions of MBP-J fusion protein were added to the wells and the
plates were incubated for 1 h at 37°C. The fraction of MBP-J bound to LamB was measured after reaction with anti-MBP antibody (at a
final dilution of 1:1,000). Goat anti-rabbit immunoglobulin G (IgG)
(heavy plus light chains [H+L]) alkaline phosphatase conjugate (final
dilution, 1:1,000) and alkaline phosphatase substrate kit (Bio-Rad)
were used for color detection of the LamB-MBP-J-anti-MBP complexes.
As shown in Fig. 3A, MBP-J/S was found to
bind tightly to LamB trimers coated to the plate. MBPwt as well as BSA
did not bind to LamB.
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FIG. 3.
ELISA binding assays. (A) Binding of MBP-J to purified
LamB trimers. Each well was coated with 150 ng of purified LamB
trimers. Increasing concentrations of MBP-J/S were added. The fraction
of MBP-J bound to LamB was revealed with anti-MBP antibody at a final
dilution of 1/1,000. (B) Inhibition of anti-LamB antibody binding to
purified LamB trimers. The plate was coated with purified LamB trimers
(150 ng/well). Increasing concentrations of MBP-J/S were added to each
well. The ELISA was carried out with anti-LamB mouse MAb E302 or MAb
E72.  , MBP-J/S hybrid;  , MBPwt;  , BSA. [c], concentration.
OD405, optical density at 405 nm.
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The capacity of bound MBP-J fusion protein to inhibit binding of
anti-LamB monoclonal antibodies (MAbs) was also tested (Fig.
3B). For
this, plates were coated with LamB trimers and incubated
with serial
dilutions of MBP-J, as described above. After several
washes in PBS,
100 µl of anti-LamB MAb (at a final dilution of
1:500) was added and
the plates were incubated at 37°C for 1 h.
The LamB-MAb
complexes were finally detected with goat anti-mouse
IgG (H+L) alkaline
phosphatase conjugate at a final dilution of
1:1,000. Two anti-LamB
MAbs (E302 and E72) against purified native
E. coli K-12
LamB protein, raised in mice and specific to cell
surface-exposed
regions of the protein, were used (
5,
6).
With both MAbs, a
strong inhibition of binding to LamB was observed
upon preincubation
with MBP-J/S. One hypothesis to account for
this inhibitory effect
would be that the phage tail tip competes
with the MAbs for the same
binding site. In agreement with this
hypothesis, previous genetic
analyses showed that the binding
sites for phages and MAbs at the
surface of LamB were distinct
but partially overlapping (
2).
However, the inhibition could
also be the result of steric
hindrance.
In vivo interactions between MBP-J hybrid and the LamB
receptor.
We next tested the effects of MBP-J binding to intact
cells on the phage receptor and the maltoporin activities of LamB and directly demonstrated binding to LamB by electron microscopy.
Inhibition of phage binding.
Different concentrations of
purified MBP-J fusion protein (in 10-µl volumes) were first incubated
at room temperature for 20 min with bacterial suspensions of the
LamB-positive strain P4X8 (in 100-µl volumes). Then 10 µl of a
dilution of phage , containing approximately 500 PFU, per mixture
was added, and the incubation was continued for 20 min. The mixtures
were finally centrifuged at 10,000 × g in a
microcentrifuge for 5 min. The number of infectious phage particles
still present in the supernatants (i.e., the unbound phage) was
determined by spreading onto indicator bacteria (Luria broth-grown
P4X8). As shown in Fig. 4, an almost complete inhibition of phage binding was obtained when MBP-J/S was
added at a final concentration of 50 µg/ml. In contrast, BSA and
MBPwt had no effect on phage binding.
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FIG. 4.
In vivo inhibition of phage binding. The one-step
extended host range derivative of wild-type phage (h°
[laboratory collection]) was used in this assay. Sensitivity to was assayed by spot tests on lawns of the LamB-positive E. coli K-12 strain, P4X8, plated by the tryptone overlay method
(1). Plates were incubated overnight at 37°C. The fraction
of phages bound to the bacteria was determined by subtracting the
number of infectious phage particles still present in the supernatants
(the fraction not bound to the bacterial pellet) from the total number
of infectious phages initially added in the assay. Purified MBPwt and
BSA were used as negative controls.
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In vivo maltose uptake.
We measured maltose uptake, as
previously described (2), at 2 µM maltose, a concentration
at which LamB is limiting for transport (3, 8). After
growth, the bacteria were preincubated on ice with 50 µg of MBPwt,
MBP-J hybrid, or BSA, for 1 h. The mixtures were further incubated
at room temperature for 30 min before the addition of
14C-labelled maltose (specific activity, 40 µCi/µmol).
The assay revealed that binding of MBP-J/S led only to a partial
(approximately two-thirds) reduction of maltose uptake (data not
shown). This result may indicate either that binding of MBP-J to LamB
only partially affected access of the sugar to its binding site within the channel or, more simply, that one-third of the LamB molecules did
not have MBP-J bound to them. This preliminary observation should be
further confirmed by using liposomal or other in vitro reconstituted systems.
Electron microscopy.
Electron microscopic analyses were
performed on the LamB-positive strain P4X8 and its LamB-negative
derivative (14). Bacteria were suspended in PBS at a
concentration of 5 × 109 bacteria/ml. A drop (20 to
50 µl) of this suspension was placed on a sheet of Parafilm. A
formvar-coated nickel grid was placed on the drop for 2 min and then,
sequentially, onto drops of the following reagents at room temperature:
PBS-0.1% glutaraldehyde for 5 min, PBS-50 mM NH4Cl for 5 min, PBS-1% BSA-1% normal goat serum for 5 min, MBP-J/S hybrid
protein at a concentration of 5 µg/ml (or the same concentration of
MBPwt) for 20 to 30 min, and anti-MBP antiserum (dilution, 1/100) for
30 min. After five washes, IgG (H+L) anti-rabbit immunoglobulin-gold
conjugate was added and the incubation was continued for 10 min. After
several washes, the grids were dried and then coated with 3 nm of
carbon in a vacuum evaporator. Specimens were examined with a Philips CM12 transmission electron microscope, under standard conditions (80 to
120 kV). As illustrated in Fig. 5,
MBP-J/S hybrid protein (Fig. 5A) but not MBPwt (Fig. 5B) bound to the
surface of the LamB-positive strain P4X8. As shown by Fig. 5C and D,
there was no nonspecific binding of MBP-J/S or MBPwt to the
LamB-negative derivative of P4X8 (14).
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FIG. 5.
Electron microscopy. Electron micrographs of bacterial
cells after immunogold labelling with anti-MBP serum. Bacteria
producing the wild-type LamB protein (P4X8) were preincubated with
either MBP-J/S hybrid (A) or MBPwt as a negative control (B). The same
assay was also performed on the LamB-negative derivative of P4X8,
designated P4X8-LamBneg. (C and D) P4X8-LamBneg
preincubated with MBP-J/S and MBPwt, respectively.
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ACKNOWLEDGMENTS |
Jiang Wang was supported by a grant from Association
Franco-Chinoise pour la Recherche Scientifique et Technique (PRA BT no. 97-04) and a grant from Centre National de la Recherche Scientifique.
We thank Colin Tinsley for careful reading of the manuscript. We thank
Pierre Gounon, Station Centrale de Microscopie Electronique, Institut
Pasteur Paris (Paris, France) for immunoelectron microscopy. Station
Centrale de Microscopie Electronique is supported by Institut Pasteur.
| |
FOOTNOTES |
*
Corresponding author. Mailing address for Alain
Charbit: Unité INSERM U411, Faculté de Médecine
Necker-Enfants Malades, 156 rue de Vaugirard, 75730 Paris Cedex 15, France. Phone: 33 1 40 61 53 76. Fax: 33 1 40 61 55 92. E-mail:
charbit{at}necker.fr. Mailing address for Maurice Hofnung:
Unité de Programmation Moléculaire et Toxicologie
Génétique, CNRS URA1444, Institut Pasteur, 25 rue du Dr.
Roux, 75724 Paris Cedex 15, France. Phone: 33 1 45 68 88 30. Fax: 33 1 45 68 88 34. E-mail: mhofnung{at}pasteur.fr.
| |
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Journal of Bacteriology, January 2000, p. 508-512, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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