Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen

Howlett, Barbara J.; Clarke, Adrienne E.

doi:10.1042/bj1970695

Cited by 42 publications

(24 citation statements)

References 33 publications

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“…The components identified by each of these antibodies ran in parallel with a major component identified on the amidoblack-stained strip. This component has a similar rel ative mobility to antigen Lpl [Smart and Knox, 1980] and glycoprotein 1 [Howlett and Clarke, 1981a], both of which were concluded to be the group-I allergen [Johnson and Marsh, 1965a, b]. It is therefore likely that these monoclonal antibodies react with one or more of the group-I 'isoallergens' [Johnson and Marsh, 1965b],…”

Section: Discussionmentioning

confidence: 99%

Development of Monoclonal Mouse Antibodies Specific for Allergenic Components in Ryegrass (Lolium perenne) Pollen

Smart

Heddle

Zola

et al. 1983

Int Arch Allergy Immunol

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The development of monoclonal mouse antibodies against ryegrass (Lolium perenne) pollen allergens is described. Hybridoma colonies secreting antibodies specific for allergenic components were detected using an enzyme-linked immunosorbent assay. Positive colonies were cloned and expanded. The pollen components with which the monoclonal antibodies interact were identified and characterised following sodium dodecyl sulphate polyacrylamide gel electrophoresis and electrophoretic transfer to nitrocellulose. In this paper six monoclonal mouse antibodies are described. Three antibodies interact with a single molecule of between 30,000 and 35,000 daltons. One antibody interacts with a component of 16,000 daltons whereas the remaining two antibodies react with more than one component, one reacting with two components at 28,000 and 30,000, and the other with five components having molecular weights between 18,000 and 71,000 daltons.

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Section: Discussionmentioning

confidence: 99%

Development of Monoclonal Mouse Antibodies Specific for Allergenic Components in Ryegrass (Lolium perenne) Pollen

Smart

Heddle

Zola

et al. 1983

Int Arch Allergy Immunol

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“…A ␤-expansin (CIM1) from soybean (Glycine max) cell cultures has been characterized partially (Downes et al, 2001) but not with respect to its potential wall extension properties. It is apparent from sequence analysis that ␣-expansins typically lack motifs for N-linked glycosylation, whereas ␤-expansins characteristically possess such motifs and have been shown to be glycosylated in the few examples studied (Marsh, 1975;Howlett and Clarke, 1981;Cottam et al, 1986;Petersen et al, 1995;Knox and Suphioglu, 1996b;Downes et al, 2001). However, we doubt that ␤-expansins from vegetative tissues cause early cell wall breakage or have a pH optimum Ͼ5, as found for Zea m 1, because acidinduced extension of native walls (not heat inactivated) from grass coleoptiles does not exhibit these properties, and it is likely that ␤-expansins are major catalysts of acid-induced extension in grass walls Li et al, 1993;Cho and Kende, 1997;Cosgrove et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Four β-Expansins (Zea m 1 Isoforms) from Maize Pollen

et al. 2003

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(P.A.B., C.V.).Four proteins with wall extension activity on grass cell walls were purified from maize (Zea mays) pollen by conventional column chromatography and high-performance liquid chromatography. Each is a basic glycoprotein (isoelectric point ϭ 9.1-9.5) of approximately 28 kD and was identified by immunoblot analysis as an isoform of Zea m 1, the major group 1 allergen of maize pollen and member of the ␤-expansin family. Four distinctive cDNAs for Zea m 1 were identified by cDNA library screening and by GenBank analysis. One pair (GenBank accession nos. AY104999 and AY104125) was much closer in sequence to well-characterized allergens such as Lol p 1 and Phl p 1 from ryegrass (Lolium perenne) and Phleum pretense, whereas a second pair was much more divergent. The N-terminal sequence and mass spectrometry fingerprint of the most abundant isoform (Zea m 1d) matched that predicted for AY197353, whereas N-terminal sequences of the other isoforms matched or nearly matched AY104999 and AY104125. Highly purified Zea m 1d induced extension of a variety of grass walls but not dicot walls. Wall extension activity of Zea m 1d was biphasic with respect to protein concentration, had a broad pH optimum between 5 and 6, required more than 50 g mL Ϫ1 for high activity, and led to cell wall breakage after only approximately 10% extension. These characteristics differ from those of ␣-expansins. Some of the distinctive properties of Zea m 1 may not be typical of ␤-expansins as a class but may relate to the specialized function of this ␤-expansin in pollen function.Expansins were first identified a decade ago as mediators of acid-induced plant cell wall extension in cucumber (Cucumis sativus) hypocotyls and oat (Avena sativa) coleoptiles (McQueen-Mason et al., 1992;Li et al., 1993) and since then have been implicated in many aspects of plant growth and development, including cell expansion, leaf organogenesis and phyllotaxy, fruit ripening, root growth, particularly during drought, cell wall disassembly, and penetration of pollen tubes in grass species (for review, see Cosgrove, 2000;Cosgrove et al., 2002). Currently, two families of expansins, named EXP (␣-expansins) and EXPB (␤-expansins), have been identified based on protein activity and sequence analysis (Shcherban et al., 1995;Cosgrove et al., 2002;Li et al., 2002). The rice (Oryza sativa) and Arabidopsis genomes also contain a small family of related genes (see http://www.bio.psu.edu/expansins/) that we have named EXPL (expansin-like) and a more distant gene named EXPR (expansin-related). It is unknown whether the proteins encoded by these distantly related genes have expansin's characteristic activity, namely a rapid induction of cell wall extension and an increase in wall stress relaxation.Although there are now many reports characterizing expansin gene expression, relatively few studies have examined the activity of expansin proteins. It seems that ␣-expansins are ubiquitous to land plants and loosen cell walls without breakdown of the major wall polysaccharides (...

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“…The first described allergens from this species were designated groups I, II, III and IV Marsh, 1965a, b, 1966a, b;Marsh, 1975], Using the recently proposed, but not yet offi cial, International Union of Immunological Societies (IUIS) nomenclature for allergens, the above allergen groups would be designated Lol pi, Lol pi I, Lol pill and Lol pIV, respectively. Group I, the major al lergen, is an acidic glycoprotein with a molecular weight (MW) of approximately 32 kD and consists of 4 isoallergenic variants [Marsh, 1975], Although a number of allergenic components have been ident ified and/or isolated from ryegrass pollen, most fit the description of one of groups I, II, III or IV [Lynch and Turner, 1974;Smart and Knox, 1980;Howlett and Clarke, 1981], Smart et al [1983] produced mon oclonal antibodies to what were probably group I and group II allergens. Other monoclonal antibodies pro duced in the same study reacted with allergenic com ponents with MWs of 28 and 30 kD.…”

Section: Introductionmentioning

confidence: 99%

A Re-examination of Ryegrass (Lolium perenne) Pollen Allergens

Ford

Baldo

1986

Int Arch Allergy Immunol

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Electroblotting of crude ryegrass pollen extracts and purified group I, II and III allergens identified 14 IgE-binding components, 8 of which were previously unrecognized. In addition to allergen groups I, II and III, which are already regarded as clinically important, and on the basis of the frequencies and intensities of IgE binding with sera from 42 ryegrass pollen-allergic patients, proteins with molecular weights (MWs) of 60, 32, 30 and 28 kD were identified as allergens of possible major clinical importance. Six other pollen components with MWs ranging from 23 to 80 kD and which reacted with IgE antibodies in the sera of 33–50% of patients, should also be viewed as proteins with potential clinical relevance for at least a proportion of the patients. The electrophoretic separation patterns of ryegrass pollen extracts in both alkaline and acid gels and IgE-probed membrane transfers produced in this study should serve as useful reference patterns for standardization purposes. In addition, the identification of the complete allergen recognition pattern by individual patients will permit safer and more effective diagnosis and therapy of ryegrass pollen sensitivities.

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Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen

Cited by 42 publications

References 33 publications

Development of Monoclonal Mouse Antibodies Specific for Allergenic Components in Ryegrass <i>(Lolium perenne)</i> Pollen

Development of Monoclonal Mouse Antibodies Specific for Allergenic Components in Ryegrass <i>(Lolium perenne)</i> Pollen

Purification and Characterization of Four β-Expansins (Zea m 1 Isoforms) from Maize Pollen

A Re-examination of Ryegrass <i>(Lolium perenne) </i>Pollen Allergens

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