Hope this really works and that they bring it to market.
Sometimes I wonder if "they" are really as dense as they seem, or if
the "nice margins"  from
chronic sinusitis and the heartburn it causes are just too attractive
for pharma to want to cure so they buy little biotech companies and
don't offer the products for sale.

After all the most cost effective medications on the planet are
vaccinations.
E-coli is the premier producer of amyloid beta and an attachment
specialist that facilitates the anchorage of everybuggy else.  There
has been a safe and effective e-coli vaccine for years, tested in
children yet, but it has never been offered for sale.
I believe that sinus infections like those we see here are rare in the
Soviet Union because they use phages to treat them that kill e-coli,
but the FDA will not allow the soviet phages refined into the country.
So the Pentagon has set up a treatment unit there.
http://www.phagetherapycenter.com/pii/PatientServlet?command=static_home
Readers of Judy's post about heparin will realize what an odd
situation this is.

This appears to be the primary publication.

Structural analysis of dispersin B, a biofilm-releasing glycoside
hydrolase from the periodontopathogen Actinobacillus
actinomycetemcomitans.
Ramasubbu N, Thomas LM, Ragunath C, Kaplan JB.

Department of Oral Biology, University of Medicine and Dentistry of
New Jersey, Newark, NJ 07103, USA. ramasun1@umdnj.edu
J Mol Biol. 2005 Jun 10;349(3):475-86. Epub 2005 Apr 14.

Bacteria in a biofilm are enmeshed in a self-synthesized extracellular
polysaccharide matrix that holds the bacteria together in a mass and
firmly attaches the bacterial mass to the underlying surface. A major
component of the extracellular polysaccharide matrix in several
phylogenetically diverse bacteria is PGA, a linear polymer of N-
acetylglucosamine residues in beta(1,6)-linkage. PGA is produced by
the Gram-negative periodontopathogen Actinobacillus
actinomycetemcomitans as well as by the Gram-positive device-
associated pathogen Staphylococcus epidermidis. We recently reported
that A.actinomycetemcomitans produces a soluble glycoside hydrolase
named dispersin B, which degrades PGA. Here, we present the crystal
structure of dispersin B at 2.0A in complex with a glycerol and an
acetate ion at the active site. The enzyme crystallizes in the
orthorhombic space group C222(1) with cell dimensions a=41.02A,
b=86.13A, c=185.77A. The core of the enzyme consists a (beta/alpha)(8)
barrel topology similar to other beta-hexosaminidases but significant
differences exist in the arrangement of loops hovering in the vicinity
of the active site. The location and interactions of the glycerol and
acetate moieties in conjunction with the sequence analysis suggest
that dispersin B cleaves beta(1,6)-linked N-acetylglucosamine polymer
using a catalytic machinery similar to other family 20 hexosaminidases
which cleave beta(1,4)-linked N-acetylglucosamine residues.

PMID: 15878175 [PubMed - indexed for MEDLINE]

There are a further 14 cites which turn up in a quick and dirty
search; much of their work seems to concern catheters and implants, on
a quick and non specialist reading the three following would seem most
directly relevant to sinus infections:-

Diffrential roles of poly-N-acetylglucosamine surface polysaccharide
and extracellular DNA in Staphylococcus aureus and Staphylococcus
epidermidis biofilms.
Izano EA, Amarante MA, Kher WB, Kaplan JB.
Medical Science Building, Room C-636, 185 S. Orange Ave., Newark, NJ
07103, USA.
Appl Environ Microbiol. 2008 Jan;74(2):470-6. Epub 2007 Nov 26.Click
here to read

Staphylococcus aureus and Staphylococcus epidermidis are major human
pathogens of increasing importance due to the dissemination of
antibiotic-resistant strains. Evidence suggests that the ability to
form matrix-encased biofilms contributes to the pathogenesis of S.
aureus and S. epidermidis. In this study, we investigated the
functions of two staphylococcal biofilm matrix polymers: poly-N-
acetylglucosamine surface polysaccharide (PNAG) and extracellular DNA
(ecDNA). We measured the ability of a PNAG-degrading enzyme (dispersin
B) and DNase I to inhibit biofilm formation, detach preformed
biofilms, and sensitize biofilms to killing by the cationic detergent
cetylpyridinium chloride (CPC) in a 96-well microtiter plate assay.
When added to growth medium, both dispersin B and DNase I inhibited
biofilm formation by both S. aureus and S. epidermidis. Dispersin B
detached preformed S. epidermidis biofilms but not S. aureus biofilms,
whereas DNase I detached S. aureus biofilms but not S. epidermidis
biofilms. Similarly, dispersin B sensitized S. epidermidis biofilms to
CPC killing, whereas DNase I sensitized S. aureus biofilms to CPC
killing. We concluded that PNAG and ecDNA play fundamentally different
structural roles in S. aureus and S. epidermidis biofilms.

PMID: 18039822 [PubMed - indexed for MEDLINE], PMCID: PMC2223269
[Available after 05/01/08]

Staphylococcus biofilm components as targets for vaccines and drugs.
Visai L, Arciola CR, Pietrocola G, Rindi S, Olivero P, Speziale P.
   University of Pavia, Department of Biochemistry, Pavia, Italy.
Int J Artif Organs. 2007 Sep;30(9):813-9.

Staphylococci have become the most common cause of nosocomial
infections, especially in patients with predisposing factors such as
indwelling or implanted foreign polymer bodies. The pathogenesis of
foreign-body associated infections with S.aureus and S. epidermidis is
mainly related to the ability of these bacteria to form thick,
adherent multilayered biofilms. In a biofilm, staphylococci are
protected against antibiotic treatment and attack from the immune
system, thus making eradication of the infections problematic. This
necessitates the discovery of novel prophylactic and therapeutic
strategies to treat these infections. In this review, we provide an
overview of staphylococcal biofilm components and discuss new possible
approaches to controlling these persistent biofilm-dwelling bacteria.

PMID: 17918127 [PubMed - indexed for MEDLINE]

Differential roles of poly-N-acetylglucosamine surface polysaccharide
and extracellular DNA in Staphylococcus aureus and Staphylococcus
epidermidis biofilms.
Izano EA, Amarante MA, Kher WB, Kaplan JB.
Medical Science Building, Room C-636, 185 S. Orange Ave., Newark, NJ
07103, USA.
Appl Environ Microbiol. 2008 Jan;74(2):470-6. Epub 2007 Nov 26.

Staphylococcus aureus and Staphylococcus epidermidis are major human
pathogens of increasing importance due to the dissemination of
antibiotic-resistant strains. Evidence suggests that the ability to
form matrix-encased biofilms contributes to the pathogenesis of S.
aureus and S. epidermidis. In this study, we investigated the
functions of two staphylococcal biofilm matrix polymers: poly-N-
acetylglucosamine surface polysaccharide (PNAG) and extracellular DNA
(ecDNA). We measured the ability of a PNAG-degrading enzyme (dispersin
B) and DNase I to inhibit biofilm formation, detach preformed
biofilms, and sensitize biofilms to killing by the cationic detergent
cetylpyridinium chloride (CPC) in a 96-well microtiter plate assay.
When added to growth medium, both dispersin B and DNase I inhibited
biofilm formation by both S. aureus and S. epidermidis. Dispersin B
detached preformed S. epidermidis biofilms but not S. aureus biofilms,
whereas DNase I detached S. aureus biofilms but not S. epidermidis
biofilms. Similarly, dispersin B sensitized S. epidermidis biofilms to
CPC killing, whereas DNase I sensitized S. aureus biofilms to CPC
killing. We concluded that PNAG and ecDNA play fundamentally different
structural roles in S. aureus and S. epidermidis biofilms.

PMID: 18039822 [PubMed - indexed for MEDLINE], PMCID: PMC2223269
[Available after 05/01/08]