Record 3 of 10 in Biological Abstracts 2000/07-2000/12

TI:  Molecular basis of IgE cross-reactivity between human
beta-casein and bovine beta-casein, a major allergen of milk.
AU:  Bernard-H {a}; Negroni-L; Chatel-J-M; Clement-G; Adel-Patient-K;
Peltre-G; Creminon-C; Wal-J-M
SO:  Molecular-Immunology. [print] February-March, 2000; 37 (3-4): 161-167.
PY:  2000
LA:  English
AB:  Twenty patients allergic to cow's milk proteins and with high
levels of specific IgE directed against bovine whole casein were
selected to evaluate reactivity of their IgE antibodies with human
beta-casein. Highly purified human and bovine beta-caseins were
prepared by selective precipitations and FPLC separation. Their
identity and purity were assessed by HPLC, analysis of amino acid
composition, sequencing of the five N-terminal amino acid residues
and immunochemical tests. Direct and indirect ELISAs were performed
using human and bovine beta-casein coated into microtiter plates and
monoclonal anti-human IgE antibody AChE labelled for revelation.
Seven sera contained specific IgE directed against human beta-casein.
Inhibition studies using native human and bovine beta-caseins as well
as bovine beta-casein-derived peptides demonstrated that, depending
on the sera, one or several common epitopes located in different
parts of the molecule were shared by the two homologous
proteins.
AN:  200000226309
UD:  20000804

Record 4 of 10 in Biological Abstracts 2000/01-2000/06

TI:  Anaphylaxis caused by the unexpected presence of casein in salmon.
AU:  Koppelman-Stef-J {a}; Wensing-Marjolein; de-Jong-Govardus-A-H;
Knulst-Andre-C
SO:  Lancet-North-American-Edition. Dec. 18-25, 1999; 354 (9196): 2136.
PY:  1999
LA:  English
AB:  A new process for restructured meat and fish has been introduced
to the market recently. Its main compound is casein, and it may
therefore endanger patients with a milk allergy.
AN:  200000128886
UD:  20000425

Record 5 of 10 in Biological Abstracts 2000/01-2000/06

TI:  A case of allergy to cow's milk hydrolysate.
AU:  Nilsson-C {a}; Oman-H; Hallden-G; Lilja-G; Lundberg-M; Harfast-B
SO:  Allergy-Copenhagen. Dec., 1999; 54 (12): 1322-1326.
PY:  1999
LA:  English
AB:  We here report a girl, now 3 years old, who has suffered from
severe food allergy since her first year of life. She was strongly
allergic to cow's milk, and had high levels of IgE antibody (AB) to
casein (210 kU/l), beta-lactoglobulin (43 kU/l), and
alpha-lactalbumin (23 kU/l) at 12 months of age. In addition, at the
same age, she showed positive (2-4+) skin prick reactions to both
unboiled and boiled formulas (Profylac, Nutramigen, and Neocate),
besides being positive in RAST to Nutramigen (0.6 kU/l). During the
first 3 years, IgE Ab levels against casein and Nutramigen increased
to 310 and 1.6 kU/l, respectively. Furthermore, at 3 years of age,
she had positive RAST to 14 of 15 tested food allergens, being
negative only to codfish. Assessment of eosinophil-related markers
revealed high total eosinophil count, increased eosinophil activity,
and a low ratio of interferon (IFN)-gamma:IL-5, indicating enhanced
IL-5 production. The food allergy was correlated to poor weight gain
and increasing problems with atopic allergy in the airways.
AN:  200000076212
UD:  20000322

Record 6 of 10 in Biological Abstracts 1999/07-1999/12

TI:  IgE cross-reactivity with caseins from different species in
humans allergic to cow's milk.
AU:  Bernard-Herve {a}; Creminon-Christophe; Negroni-Luc;
Peltre-Gabriel; Wal-Jean-Michel
SO:  Food-and-Agricultural-Immunology. March, 1999; 11 (1): 101-111.
PY:  1999
LA:  English
AB:  Fifty-eight sera from humans allergic to cow s milk proteins
were analysed for the specificity of their IgE response to the whole
casein fraction of milk from different ruminant and non-ruminant
species (e.g. cow, sheep, goat, rabbit and rat). IgE-specific
responses were determined by an enzyme allergosorbent test using the
purified casein fractions as immobilized antigen and an anti-human
IgE monoclonal antibody labelled with acetylcholinesterase. Co-and/or
cross-sensitizations to caseins of the different ruminant species
occurred extensively, though IgE responses to ovine and caprine
casein appeared to be lower than that obtained with bovine casein.
Cross-reactivity is suggested by the significant reactivity of rat
and rabbit casein toward human IgE. In terms of specificity and
intensity, the IgE response to caseins demonstrates a great
variability. Structural homologies in caseins of such different
species, that can share common epitopes for the IgE of some patients,
suggest that prevention of cow s milk allergy cannot be achieved by
using milk from other species as substitutes.
AN:  199900193713
UD:  19990723