Antigens Common to Hosts and Parasites

DeVay, J. E.; Adler, H. E.

doi:10.1146/annurev.mi.30.100176.001051

Cited by 58 publications

(18 citation statements)

References 71 publications

(126 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ability of Bdellovibrio to disguise itself within a 'host-like phenotype' could represent a step towards the evolution of a mechanism to escape the host's defense mechanisms. In fact, the appropriation of host proteins by Bdellovibrio may provide a model, useful for the interpretation of the widespread sharing of antigens between hosts and parasites (Damian, 1964;De Vay and Adler, 1976), not only as a consequence of evolutionary convergence of proteins but also via direct uptake of host antigens, as described in Schistosoma (Smithers et al, 1969;Clegg et al, 1971;Sher et al, 1978;Bloom, 1979).…”

Section: Discussionmentioning

confidence: 99%

Molecular parasitism in the Escherichia coli-Bdellovibrio bacteriovorus system: translocation of the matrix protein from the host to the parasite outer membrane.

Guerrini¹,

Romano²,

Valenzi³

et al. 1982

The EMBO Journal

View full text Add to dashboard Cite

During the intracellular maturation in Escherichia coli of the parasite Bdellovibrio bacteriovorus the outer membrane, major protein I of E. coli (i.e., the matrix protein) becomes associated with the outer membrane of the emerging parasite cells. The binding properties of this protein with the outer membrane of the host and of the parasite are identical. An analogous phenomenon also occurs during Bdellovibrio parasitism on Klebsiella pneumoniae and on Salmonella typhimurium. Possible roles for this scavenging action of Bdellovibrio, and similar phenomena in other parasitic systems, are discussed.

show abstract

Section: Discussionmentioning

confidence: 99%

Molecular parasitism in the Escherichia coli-Bdellovibrio bacteriovorus system: translocation of the matrix protein from the host to the parasite outer membrane.

Guerrini¹,

Romano²,

Valenzi³

et al. 1982

The EMBO Journal

View full text Add to dashboard Cite

show abstract

“…Pretreatment of Gladiolus stigmata with Con A prevented compatible pollen tubes from penetrating (10). There is also considerable evidence that the specificity of host-symbiont interactions is determined by lectin binding (1,3,4,8,15,21). Gamborg and Miller (5) suggested that lectins may be useful for protoplast aggregation which in turn would facilitate fusion.…”

mentioning

confidence: 99%

Plant Protoplast Agglutination by Lectins

Larkin¹

1978

Plant Physiol.

View full text Add to dashboard Cite

Coicanavain A, soybean (Glyce max L.) ectin, castor bea (Rkhns communis L.) lectn, and peanut (Machis hypogaea L.) lectin were able to agglutinate protoplasts prepared from a variety of plant species. The seven other lectins tried were unable to agglutinate those protoplasts tested. Protoplasts prepared from 11 species were used. The lectins examined were not able to differentiate among protoplasts of different species.Recently there has been some interest in the effects of plant lectins on plant cell systems. Phaseolus vulgaris lectin was shown to have a mitogenic effect on tomato callus cells (13) and barley and pea root tip cells (17). Soybean lectin was mitogenic for soybean callus cells (9). PHA2 and Con A both stimulate Lilium pollen germination (18). Golynskaya et al. (7) found hemagglutinins in Primula stigmata which also effected pollen tube growth. Pretreatment of Gladiolus stigmata with Con A prevented compatible pollen tubes from penetrating (10). There is also considerable evidence that the specificity of host-symbiont interactions is determined by lectin binding (1,3,4,8,15,21). Gamborg and Miller (5) suggested that lectins may be useful for protoplast aggregation which in turn would facilitate fusion. Since then Glimelius et al. (6) reported the agglutination of carrot culture cell protoplasts by Con A. They observed inhibition of the agglutination by methyl-a-D-glucoside and a great reduction of agglutination using glutaraldehyde-fixed protoplasts. Low temperature (4 C) limited agglutination and higher cell densities favored higher agglutination percentages. Burgess and Linstead (2) confirmed the ability of Con A to interact with protoplast surfaces. Using Con A conjugated with colloidal gold they demonstrated both specific binding (inhibited by 0.1 M a-methyl mannoside) to plasmalemma of Vitis vinifera culture and tobacco leaf protoplasts, and also nonspecific binding to amorphous material near the plasmalemma. The ability of plant lectins to interact with plasmalemma may be of significance to their physiological role. Ruesink (16) and Williamson et aL (19,20) (200 g, uncooked) were milled, defatted with 500 ml of petroleum ether, and air-dried. A suspension in 0.9% (w/v) NaCl was stirred for 3 hr and the insoluble matter removed twice by centrifugation. (NH4)SO4 was added to 60% (w/v) saturation and the centrifuged pellet redissolved in 110 ml of 0.9%/v (w/v) NaCl and dialyzed against 0.9%o (w/v) NaCl for 24 hr with one change of saline. One sample was also dialyzed against OSI (pH 7.2) for 24 hr.Vicia faba beans (40 g) were milled, defatted with 300 ml of petroleum ether, and dried in air. The flour was suspended and stirred for I hr in 200 ml of 0.9% (w/v) NaCl. The centrifuged sediment was discarded. The supernatant was fractionated by (NH4)SO4 precipitation into the 0 to 48%, 48 to 65%, 65 to 80%o and 80 to 100%o (w/v)

show abstract

“…The seeming alteration in phytopathogenic specialization resulting from repeated passage of xanthomonads through heterologous host plants (Dye, 1958;Shackleton, 1966) might now be reconsidered in the contexts of the common antigen work (DeVay and Adler, 1976) and the constant "evolution" of "new" Xanthomonas nomenspecies. In doing so, it is important to bear in mind that the various Xanthomonas nomenspecies are phenetic ally similar entities that differ from one another mainly in phytopathogenic specialization under field and conventional experimental conditions, and in partial polynucleotide sequence homology; they differ also in some other ways (e.g., serology, electrophoretic mobility of proteins, common antigens), which might derive from or pertain to the aforementioned two major differences.…”

Section: Phytopathogenic Specialization ( "Host Specificity") In Xantmentioning

confidence: 99%

The Genus Xanthomonas

Starr¹

1981

The Prokaryotes

View full text Add to dashboard Cite

Antigens Common to Hosts and Parasites

Abstract: If we search for factors of (disease) resistance. they are legion; if we search for factors of susceptibility. our search is narrowed down to certain varieties of a few. very closely related species of plants. and to the diff erences between closely related varieties.

Cited by 58 publications

References 71 publications

Molecular parasitism in the Escherichia coli-Bdellovibrio bacteriovorus system: translocation of the matrix protein from the host to the parasite outer membrane.

Molecular parasitism in the Escherichia coli-Bdellovibrio bacteriovorus system: translocation of the matrix protein from the host to the parasite outer membrane.

Plant Protoplast Agglutination by Lectins

The Genus Xanthomonas

Contact Info

Product

Resources

About