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PubMed1971

Temperature-dependent surface changes in cells infected or transformed by a thermosensitive mutant of polyoma virus.

Infection of BALB/3T3 cells by polyoma virus causes an alteration in the cell surface, characterized by enhanced agglutination of the cells by wheat germ agglutinin or concanavalin A. Infection by the thermosensitive mutant of polyoma, ts-3, causes the cell surface alteration at the permissive temperature, but not at the nonpermissive temperature. The cell surface alteration requires cellular DNA synthesis, but not viral DNA synthesis. BHK cells transformed by ts-3 show the surface alteration when grown at the permissive temperature, but not when grown at the nonpermissive temperature. It is concluded that the surface alteration in transformed cells is under the control of a viral gene.

Agglutination↗
PubMed1977

Demonstration of enterobacterial common antigen by bacterial agglutination.

Potent antisera against the enterobacterial common antigen (ECA) agglutinate R bacteria of the Enterobacteriaceae family that possess unimpaired R-core structures of the Escherichia coli R1 or E. coli R4 core type. In these strains, known to be ECA immunogenic, ECA is most probably linked to the lipopolysaccharide R core. R mutants of other core types (e.g., Salmonella Ra, E. coli R2 or R3) or R mutants with incomplete core structures of the E. coli R1 type, as well as an rfaL mutant deficient in the O-translocase system, agglutinate to a much lesser extent or not at all. All the later mutants are nonimmunogenic; they possess the ECA in a free form, not linked to the R core. None of the S forms tested from many different enterobacterial genera was found to be agglutinable with the ECA antiserum. The dynamics of the ECA agglutinin formation in rabbits parallels the ECA hemagglutinin formation, indicating that the same antibody class might be involved in bacterial agglutination and hemagglutination.

Agglutination↗
PubMed1981

Transplantation for acute leukaemia with HLA-A and B nonidentical parental marrow cells fractionated with soybean agglutinin and sheep red blood cells.

A new procedure for enrichment of marrow precursors and removal of T lymphocytes from large volumes of human bone marrow, involving initial differential agglutination of T lymphocytes and mature marrow elements with soybean agglutinin, followed by rosetting with sheep red blood cells, was used to fractionate marrow cells from an HLA-A, B, DR non-identical, MLC non-reactive, paternal donor for transplantation into an infant with acute leukaemia. This transplant became completely engrafted and resulted in full recovery of normal, donor-derived haematopoietic function without graft-versus-host disease, sustained for 11 weeks after transplantation, at which time the patient's leukaemia recurred. Subsequently, the patient received chemotherapy and achieved a remission with regeneration of normal marrow cells of donor origin. The patient's course demonstrated the potential of lectin-separated marrow grafts to restore durable haematopoiesis, without graft versus host disease, in a lethally irradiated allogeneic host.

Agglutinins↗
PubMed2002

Role of Fig2p in agglutination in Saccharomyces cerevisiae.

In W303-derived strains, disruption of FIG2 increased agglutinability of alpha cells, but not a cells, and did not alter expression of alpha-agglutinin, binding of 125I-labeled alpha-agglutinin, or mating efficiency. Fig2p overexpression led to alpha-cell-specfic suppression of agglutinability. These results imply that Fig2p is an indirect masker of the active sites in alpha-agglutinin.

Cell Adhesion↗
PubMed1985

The platelet activation induced by wheat germ agglutinin.

In human platelets, wheat germ agglutinin (WGA) induced serotonin release without cell agglutination. WGA induced the phosphorylation of both 40-kDa and 20-kDa proteins in a parallel manner, and at least, the phosphorylation of 40-kDa protein was preceded by transient formation of endogenous diacylglycerol (DG) accompanied by a decrease in phosphatidylinositol (PI). Both phosphorylation of these two proteins and serotonin release were inhibited by prior treatment of platelets with dibutyryl cyclic AMP, W-7, or TMB-8. These results suggest that both phosphatidylinositol turnover and Ca2+ mobilization play an essential role in WGA-induced platelet activation.

Aminoquinolines↗
PubMed1983

Differential agglutination of P388 adriamycin-sensitive and P388 adriamycin-resistant leukemia cells.

Cell surface modification was studied in a subline of murine leukemia resistant to adriamycin (P388/ADR). Lectin-induced agglutination was used as a probe. Agglutination was studied using two plant lectins, wheat germ agglutinin (WGA) and Ricinus communis agglutinin-I (RCA-I). A 7-fold higher amount of WGA and 14-fold higher amount of RCA-I were required to bring about minimum agglutination of P388/S as compared to P388/ADR. The present studies clearly indicate a change in the plasma membrane of P388/ADR cells.

Agglutination↗
PubMed1995

Hemagglutinins in fungus extracts and their blood group specificity.

A total of 833 fungi harvested from 1977 to 1994 were tested and 422 extracts (47.8%) produced hemagglutination of human red cells. The lectins in fungus extracts which showed blood-group-specific or related reactions were partially purified by ammonium sulfate precipitation and gel filtration on a Sephadex G-100 column. Anti-H-like agglutinins were found in extracts of Pleurocybella porrigens, Naematoloma sublateritium and Pholiota squarrosa. These extracts agglutinated strongly with human group O red cells and rather weakly with A and B cells. Anti-A agglutinins were found in extracts of Hohenbuehelia serotina, Paxillus panuoides, Melanoleuca melaleuca and Hygrophorus capreolarius. The extract of Clavulinopsis fusiformis contained anti-B agglutinin. The ABH reactivities of the extracts were cofirmed by an agglutination inhibition test with ABH secretor saliva and blood group substances from human gastric linings and by the destruction of inhibiting activity using blood-group-specific decomposing enzymes. L-Fucose was the most active inhibiting monosacharide of anti-H-like agglutinins. The reaction of anti-A agglutinins was strongly inhibited by N-acetyl-D-galactosamine. D-Galactose and raffinose and melibiose which contain alpha-galactosyl residues were potent inhibitors of C. fusiformis agglutinin.

ABO Blood-Group System↗
PubMed1978

Comparison of selected diagnostic tests for detection of motile Aeromonas septicemia in fish.

Cultural isolation, slide agglutination (SA), tube agglutination (TA), microagglutination (MA), and fluorescent antibody (FA) techniqes were compared as methods for detecting motile aeromonas septicemia in channel catfish (Ictalurus punctatus). Tests were conducted on naturally infected fish from feral populations and commercial sources, as well as on fish which were experimentally infected with a virulent culture of Aeromonas hydrophila. Increased levels of specific serum agglutinins to A hydrophila were demonstrable only in fish from whose blood the organism could be recovered. It was concluded that the SA procedure was an effective diagnostic test which would be most useful under field conditions. Under laboratory conditions, the TA, MA, and FA procedures were found to be equally effective in detecting the level of serum agglutinins to A hydrophila. The FA procedure, however, was more sensitive than any of the agglutination procedures and could be performed in less time than TA or MA.

Aeromonas↗
PubMedDate not supplied

Expression of the aggA locus of Pseudomonas putida in vitro and in planta as detected by the reporter gene, xylE.

In vitro agglutinability by Pseudomonas putida, isolate Corvallis, with a plant root surface agglutinin is correlated with rapid adhesion of cells of the fluorescent pseudomonad to bean (Phaseolus vulgaris) root surfaces. Agglutinability in P. putida cells is regulated by nutrient status as well as growth phase. Cells grown in three different nutrient complex media are agglutinable at early and mid-late logarithmic phase but become nonagglutinable at stationary phase. Cells grown in a minimal medium are weakly agglutinable, but the addition of lysine, aspartic acid, or histidine increases agglutinability. Cells in the same minimal medium supplemented with bean root surface components grow in a highly agglutinated state. Previous data indicate both agglutination and rapid adhesion to roots by P. putida Corvallis involves the aggA locus, which contains two putative open reading frames (ORF), ORF-AGG1 and ORFAGG2, on complementary strands. Sequence and deletion analyses suggest ORFAGG1 is the most probable ORF responsible for agglutination and adhesion. Chimeric fusion of an Escherichia coli lac promoter with ORFAGG1, but not with ORFAGG2, complemented agglutinability of an aggA::Tn5 P. putida Agg mutant, providing further evidence that ORFAGG1, not ORFAGG2, is responsible for agglutination. Heterologous expression of ORFAGG1 yields a 50-kDa precursor and a 48-kDa mature periplasmic protein. Fusions of ORFAGG1 and ORFAGG2 to the reporter gene, xylE, and detection of the reporter enzyme, catechol-2,3-oxygenase reveal an active promoter in the 5' noncoding region of ORFAGG1. The ORFAGG1 promoter is active during growth of the cells in liquid culture and is regulated by growth medium. Greatest activity of the catechol-2,3-oxygenase is observed in stationary phase when the cells are nonagglutinable. Expression of the ORFAGG1 promoter is detected in P. putida cells extracted from the root surface of bean at 48 and 72 hr after inoculation.

Agglutination↗
PubMed1983

Fertilizing capacity and sperm antibodies in vasovasostomized men.

In order to explain the discrepancy between the patency rate (80%) and the pregnancy rate (46%) in a series of vasovasostomies, attention was focused on a group of patients who became normospermic. The mean age at vasectomy, the duration of vasobstruction, and the parameters of semen analysis were not different for those couples who achieved a pregnancy (n = 8), compared with those couples without pregnancy (n = 7). In the group with pregnancy, six of the eight patients had low titers of serum agglutinins (absent to 1:32), and the fertilizing capacity of their spermatozoa was normal. None had immobilizing antibodies. In the group without pregnancy, six of the seven patients had elevated serum agglutinins (greater than 1:256), and four had agglutinating antibodies in their seminal plasma as well as serum immobilizing antibodies. The spermatozoa of seven patients failed to fertilize zona-free hamster ova. It is concluded that a loss of fertilizing ability of the spermatozoa due to sperm antibodies is an important cause of infertility in vasovasostomized men.

Adult↗
PubMed1991

The AGA1 product is involved in cell surface attachment of the Saccharomyces cerevisiae cell adhesion glycoprotein a-agglutinin.

Saccharomyces cerevisiae a and alpha cells express the complementary cell surface glycoproteins a-agglutinin and alpha-agglutinin, respectively, which interact with one another to promote cellular aggregation during mating. Treatment of S. cerevisiae a cells with reducing agents releases the binding subunit of a-agglutinin, which has been purified and characterized; little biochemical information on the overall structure of a-agglutinin is available. To characterise a-agglutinin structure and function, we have used a genetic approach to clone an a-agglutinin structural gene (AGAI). Mutants with a-specific agglutination defects were isolated, the majority of which fell into a single complementation group, called aga1. The aga1 mutants showed wild-type pheromone production and response, efficient mating on solid medium, and a mating defect in liquid medium; these phenotypes are characteristic of agglutinin mutants. The AGA1 gene was cloned by complementation; the gene sequence indicated that it could encode a protein of 725 amino acids with high serine and threonine content, a putative N-terminal signal sequence, and a C-terminal hydrophobic sequence similar to signals for the attachment to glycosyl phosphatidylinositol anchors. Active a-agglutinin binding subunit is secreted by aga1 mutants, indicating that AGA1 is involved in cells surface attachment of a-agglutinin. This result suggests that AGA1 encodes a protein with functional similarity to the core subunits of a-agglutinin analogs from other budding yeasts. Unexpectedly, the AGA1 transcript was expressed and induced by pheromone in both a and alpha cells, suggesting that the a-specific expression of active a-agglutinin results only from a-specific regulation of the a-agglutinin binding subunit.

Agglutination↗
PubMed1980

Interactions of phospholipid vesicles with rat hepatocytes in vitro. Influence of vesicle-incorporated glycolipids.

We examined the interaction of glycolipid-containing phospholipid vesicles with rat hepatocytes in vitro. Incorporation of either N-lignoceroyldihydrolactocerebroside or the monosialoganglioside, GM1, enhanced liposomal lipid uptake 4-5-fold as judged by the uptake of radioactive phosphatidylcholine as a vesicle marker. Cerebroside enhanced phospholipid uptake only when incorporated into dimyristoyl, but not into egg phosphatidylcholine vesicles. The lack of cerebroside effect in egg phosphatidylcholine-containing vesicles appeared to be due to a limited exposure of the carbohydrate part of the glycolipid as suggested by the reduced agglutinability of those vesicles by Ricinus communis agglutinin. In contrast to the results with radioactive phosphatidylcholine, we observed only a 20% increase in vesicle-cell association as a result of glycolipid incorporation, when a trace amount of [14C]cholesteryloleate served as a marker of the liposomal lipids or when using the fluorescent dye, carboxyfluorescein, as a marker of the aqueous space of the vesicles. By the same token, intracellular delivery of vesicle-contents was only slightly enhanced (approx. 10%). The discrepancy between the association with the cells of phosphatidylcholine on the one hand and cholesteryloleate or entrapped marker on the other suggests different mechanisms of uptake for these markers. Our results are compatible with the notion that the main effect of incorporation of glycolipids into the vesicle is the enhancement of exchange or transfer of phospholipid molecules between vesicles and cells. Incubation of the cells with galactose or lactose, prior to addition of vesicles, suggests that this enhanced phospholipid exchange or transfer involves specific recognition of the terminal galactose residues of the glycolipid vesicles by a receptor present on the plasma membranes of hepatocytes.

Animals↗
PubMed1979

Cold agglutinin disease. Report of a case.

Cold agglutinin disease is an autoimmune hemolytic anemia with varying causes. Two major types are recognized, with different clinical manifestations. Cold agglutinins are circulating antibodies capable of erythrocyte agglutination. However, the reaction is readily reversible. Treatment of the disease is variable. A case is presented to illustrate that minor oral surgical procedures are feasible, provided the proper precautions are taken.

Alveoloplasty↗
PubMed2004

Synthesis and lectin binding ability of glycosamino acid-calixarenes exposing GlcNAc clusters.

Novel calix[4 or 8]arene-based glycoconjugates exposing terminal N-acetyl-D-glucosamine clusters have been synthesized using amino acid-calixarenes as building blocks. The obtained glycosamino acid-calixarenes 9b-14b have lectin-binding ability and amplified inhibitory effects on erythrocyte agglutination induced by wheat germ (Triticum vulgaris) agglutinin (WGA). The inhibitory ability is dependent on the presence of the spacer and on the shape and rigidity of the calixarene skeleton.

Acetylglucosamine↗
PubMed1998

Lectin binding in normal, scarred, and keratoconus corneas.

PURPOSE: Keratoconus is characterized by central thinning and an increased curvature of cornea. Scarring of cornea accompanies the disease as it proceeds, and the ultimate treatment is keratoplasty. The pathogenesis of keratoconus is still unknown, and therefore we studied normal, keratoconus, and scarred corneas by a panel of lectin conjugates. METHODS: The following lectin conjugates were used: concanavalin A (Con A), Dolichos biflorus agglutinin (DBA), peanut agglutinin (PNA), Ulex europaeus agglutinin (UEA-I), wheat-germ agglutinin (WGA), Helix aspersa agglutinin (HAA), Psophocarpus tetragonolobus agglutinin (PTA), soybean agglutinin (SBA), Griffonia simplicifolia agglutinin-I-B4 (GSA-I-B4), Ricinus communis agglutinin (RCA-I), and Lotus tetragonolobus agglutin (LTA) conjugates, differently recognizing saccharide residues in glycoconjugates. RESULTS: One of the keratoconus corneas was badly scarred, whereas no scars were seen on histopathologic examination in other keratoconus corneas. In all keratoconus corneas, discontinuities or breaks (defects) were seen in the Bowman's layer. DBA and HAA conjugates, both blood group A reactive, reacted with corneal and conjunctival epithelium, blood vessels, and endothelium in blood groups A and AB. The blood group B-reactive GSA-I-B4 conjugate reacted with corneal and conjunctival epithelium, blood vessels, and endothelium only in specimens with blood group B. The blood group O-reactive UEA-I conjugate revealed the apical epithelial cells and blood vessels in all blood groups, whereas LTA conjugate, also blood group O reactive, reacted with all structures in cornea and conjunctiva despite blood groups. HAA and DBA conjugates reacted with defects in keratoconus corneas, SBA and RCA-I conjugates with defect area in keratoconus and scar region in scarred corneas, and PNA and WGA conjugates with the scar region of scarred keratoconus and scarred corneas. No other differences in the binding of lectins between normal, scarred, and keratoconus corneas were seen. CONCLUSIONS: The results indicate that the blood group status influences lectin binding in cornea. Furthermore, the difference in lectin binding to defects in keratoconus corneas (HAA and DBA conjugates) and to scar regions in scarred corneas (PNA and WGA conjugates) suggests that the defects in keratoconus are not solely the results of scarring.

Adolescent↗
PubMed1978

A simple immunofluorescence test for the detection of platelet antibodies.

Immunofluorescence tests on platelets have always been hampered by nonspecific fluorescence caused by non-immunological binding of plasma proteins to the platelet membrane. It was found that this could be easily overcome by fixation of the cells with paraformaldehyde (PFA). By using PFA-fixed platelets, a simple method for the detection of platelet antibodies, the platelet suspension immunofluorescence test (PSIFT) was developed. PFA fixation did not alter or inactivate the platelet antigens tested. Platelet-reactive antibodies detected specifically with the PSIFT included platelet-specific agglutinins of the IgM class, non-agglutinating platelet-specific antibodies of the IgG class, drug-dependent platelet antibodies, HLA antibodies, as well as anti-A and anti-B antibodies. The sensitivity of the new test was satisfactory, as was its reproducibility. Measurement of platelet immunofluorescence was possible in a continuous flow microfluorometer, making a principle, quantitation of platelet antibodies and antigens possible.

Antibodies↗