I have been somewhat overwhelmed by the mostly positive response to my more
recent posts.  And carol thank you for your well-written support.  I do want
you'all to know that if I were to pick an issue in breastfeeding it would not
have been genetic engineering of human milk.  My main focus was and still is
the current "madness" in regard to hiv and breastfeeding.  But here I am...

Certainly glowing in the praise and also feeling the criticism.  I think the
criticism is just as important as the praise.  A critic helps us grow and
stretch to find the truth.  And I'll be honest that finding the truth in all
of this has been difficult.

I wish Mary that you could be more specific about what you view as hogwash.
It is very difficult for me to respond without knowing what it is that I am
writing is wrong.  I am under the impression that you believe that
biotechnology is not currently capable of genetic engineering human milk
components.  I believe that recombinant human lactoferrin was first
genetically engineered in 1985. But I am not sure because statements by
various companies conflict with one another.  But this is a news item from
from the University of Buffalo--note the date, production sceduled for 2
years hence--1997!!

" UB Biologists Clone, Express Key Iron-Binding Protein With Commercial
Promise

Release date: Friday, June 9, 1995
Contact: Ellen Goldbaum, [log in to unmask]
Phone: 716-645-2626
Fax: 716-645-3765

BUFFALO, N.Y. -- A powerful human protein that destroys pathogens by
depriving them of the iron they need to grow has been cloned, expressed and
purified by University at Buffalo biologists, who have filed for patent
protection on the research.

Recombinant lactoferrin has commercial potential for products ranging from an
antimicrobial agent to an improved infant formula.

The research was funded by FerroDynamics, Inc., a biotechnology company in
Houston that has licensed worldwide rights to recombinant human lactoferrin
and its commercial uses from the University at Buffalo.

Found in most physiological fluids, such as tears, mucus and mother's milk,
the protein's critical feature is its ability to bind iron, making much of it
unavailable to invading pathogens.

"Lactoferrin's high affinity for iron makes it a key player in the human
immune system," explained Darrell Doyle, Ph.D., professor of biological
sciences at UB who directed the research.

"It's a natural antibiotic," he said.

But cloning the human gene for lactoferrin has not been easy.

"For years, people have tried unsuccessfully to clone a full-length
lactoferrin gene," noted Marian L. Kruzel, Ph.D., president of FerroDynamics.

Cloning was difficult because of the large fragment of DNA that had to be
expressed: The gene that codes for lactoferrin is about 2,000 base pairs
long.

Identifying the right expression system for reproducing the protein also was
critical.

Because the right kinds of sugars are necessary for the protein to function
properly, common expression systems like bacteria, which do not glycosylate
proteins (add sugars to them), cannot be used.

The UB team was successful when Paul Gollnick, Ph.D., assistant professor of
biological sciences at UB, and Tomasz Kurecki, Ph.D., senior research support
specialist, used the PCR (polymerase chain reaction) method to clone the
full-length human lactoferrin gene.

Using a picha pastoris yeast expression system, FerroDynamics confirmed the
ability to produce human lactoferrin on the laboratory scale.

Now in the process of scaling up from pilot production of lactoferrin,
FerroDynamics expects to have its first product on the market within two
years. The company's primary focus is the market for topical antimicrobial
products.

At the first sign of infection, white blood cells release lactoferrin, which
fights bacterial invaders by depriving them of the iron critical to their
growth.

Unlike currently available antibiotics, each of which is designed to combat a
specific type or group of bacteria, lactoferrin is nonspecific.

According to Kruzel, that provides an important advantage.

"Over time, bacteria being treated with antibiotics such as penicillin or
streptomycin can evolve strains that are resistant to specific
characteristics in those drugs," he explained.

But human lactoferrin binds to, or sequesters, the iron of all pathogens.

"Without iron, pathogens cannot survive," he said.

Among the other lactoferrin products FerroDynamics expects to market is an
additive to make baby formula more like human milk.

Studies of breast-fed infants have shown that babies fed human milk, which is
rich in lactoferrin, absorb iron from it much more efficiently than babies
fed infant formulas fortified with iron, Doyle explained.

Other products that are now possible based on the UB research include food
preservatives, dietary supplements and skin-care products."

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