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,
* Department of Microbiology, Yonsei University College of Medicine, Seoul, Korea;
Department of Chemistry, University of Rochester, Rochester, NY 14642; and Departments of
Pathology and
Microbiology, School of Medicine, Division of Laboratory Medicine, University of Alabama, Birmingham, AL 35294
Two groups of bacteriophage clones displaying the antigenic
properties of serotype 6B pneumococcal capsular polysaccharide (PS)
were obtained from different phage libraries expressing random
heptameric peptides. One group, biopanned with a mouse mAb (Hyp6BM1),
is comprised of 17 phage clones expressing 10 unique sequences of
linear peptides. The other group, selected with another mAb (Hyp6BM8),
contained six clones, all of which expressed the identical circular
peptide. Phage clones expressing the linear peptides (e.g., PhaM1L3)
bound only to Hyp6BM1, but not other 6B PS-specific mAb, and their
binding could be inhibited with pneumococcal capsular type 6B PS only.
In contrast, a phage clone expressing the circular peptide (PhaM8C1)
cross-reacted with several other 6B PS-specific mAbs, and their binding
could be inhibited with pneumococcal capsular PS of 6A and 6B
serotypes. Two short peptides, PepM1L3 and PepM8C1, reflecting the
peptide inserts of the corresponding phage clones, could inhibit the
binding of the two clones to their respective mAb. Interestingly, the
peptide insert in PhaM8C1 was identical to that in PhaB3C4, a
previously reported mimotope of 
(2
8) polysialic acid,
Neisseria meningitidis group B PS. Indeed, PhaM8C1 bound
to HmenB3 (a meningococcal Ab), and their association could be
inhibited with (2–8) polysialic acid, but not with 6B PS.
Conversely, (2–8) polysialic acid could not inhibit the binding of
PhaM8C1 to Hyp6BM8. The two-dimensional nuclear magnetic resonance
studies indicate that PepM8C1 peptide can assume several conformations
in solution. The ability of this peptide to assume multiple
conformations might account for its ability to mimic more than one Ag
type.
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