778:. It is used for qualitative and quantitative determination of both antigen and antibody. It involves the reaction of soluble antigen with soluble antibodies to form large interlocking aggravated called lattice. It occurs in two distinct stages. Firstly, the antigen and antibody rapidly form antigen-antibody complexes within few seconds and this is followed by a slower reaction in which the antibody-antigen complexes forms lattices that precipitate from the solution.
122:
57:. The antigens and antibodies combine by a process called agglutination. It is the fundamental reaction in the body by which the body is protected from complex foreign molecules, such as pathogens and their chemical toxins. In the blood, the antigens are specifically and with high affinity bound by antibodies to form an antigen-antibody complex. The immune complex is then transported to cellular systems where it can be destroyed or deactivated.
155:
113:
the blood. There are many antibodies and each is specific for a particular type of antigen. Thus immune response in acquired immunity is due to the precise binding of antigens to antibody. Only very small area of the antigens and antibody molecules actually interact through complementary binding sites, called epitopes in antigens and paratopes in antibody.
728:
Normally antibodies can detect and differentiate molecules from outside of the body and those produced inside the body as a result of cellular activities. Self molecules as ignored by the immune system. However, in certain conditions, the antibodies recognise self molecules as antigens and triggers
193:
are all known to be involved depending on the interaction sites. Non-covalent bonds between antibody and antigen can also be mediated by interfacial water molecules. Such indirect bonds can contribute to the phenomenon of cross-reactivity, i.e. the recognition of different but related antigens by a
112:
Immunity developed as an individual is exposed to antigens is called adaptive or acquired immunity, in contrast to immunity developed at birth, which is innate immunity. Acquired immunity depends upon the interaction between antigens and a group of proteins called antibodies produced by B cells of
99:
The principles of specificity and cross-reactivity of the antigen-antibody interaction are useful in clinical laboratory for diagnostic purposes. One basic application is determination of ABO blood group. It is also used as a molecular technique for infection with different pathogens, such as HIV,
158:
Structure of hen egg lysozyme (HEL) antigen. (A) The 3-D structure of HEL (CPK representation) together with three Abs (ribbon representation). (B) The structure of HEL colored according to the same three epitopes as in (A). (C) The structure of HEL colored according to the epitopes predicted by
150:
these are roughly from residues 28 to 35, from 49 to 59, and from 92 to 103, respectively. HV3 is the most variable part. Thus these regions may be part of a paratope, the part of an antibody that recognizes and binds to an antigen. The rest of the V region between the hypervariable regions are
712:
for that antigen. Since antibodies are bivalent or polyvalent, this is the sum of the strengths of individual antibody-antigen interactions. The strength of an individual interaction between a single binding site on an antibody and its target epitope is termed the affinity of that interaction.
566:. However, these equations are applicable only to a single epitope binding, i.e. one antigen on one antibody. Since the antibody necessarily has two paratopes, and in many circumstances complex binding occurs, the multiple binding equilibrium can be summed up as:
699:
704:
where, at equilibrium, c is the concentration of free ligand, r represents the ratio of the concentration of bound ligand to total antibody concentration and n is the maximum number of binding sites per antibody molecule (the antibody valence).
557:
425:
1124:
Braden, BC; Dall'Acqua, W; Eisenstein, E; Fields, BA; Goldbaum, FA; Malchiodi, EL; Mariuzza, RA; Schwarz, FP; Ysern, X; Poljak, RJ (1995). "Protein motion and lock and key complementarity in antigen-antibody reactions".
137:
polypeptide. This region, called the variable (V) domain, is composed of amino acid sequences that define each type of antibody and their binding affinity to an antigen. The combined sequence of variable light chain
67:
There are several types of antibodies and antigens, and each antibody is capable of binding only to a specific antigen. The specificity of the binding is due to specific chemical constitution of each antibody. The
1572:
Taylor, Charles W.; Chakrabarty, Subhas; Schauder, Keith S.; Yeoman, Lynn C. (1983). "Identification of
Cytosolic Antigens from GW-39 Adenocarcinoma Cells by Crossed Immunoelectrophoresis and Immunofluorescence".
733:
depending on the type of antigens and antibodies involved. Such conditions are always harmful and sometimes deadly. The exact nature of antibody-antigen interaction in autoimmune disease is not yet understood.
202:
Antigen and antibody interact through a high affinity binding much like lock and key. A dynamic equilibrium exists for the binding. For example, the reaction is a reversible one, and can be expressed as:
2005:
1209:
Oda, Masayuki; Uchiyama, Susumu; Noda, Masanori; Nishi, Yoshinori; Koga, Maiko; Mayanagi, Kouta; Robinson, Carol V.; Fukui, Kiichi; Kobayashi, Yuji; Morikawa, Kosuke; Azuma, Takachika (2009).
789:
It acts on antigen-antibody reaction in which the antibodies cross-link particulate antigens resulting in the visible clumping of the particle. There are two types, namely active and passive
1081:
Lisova, O; Belkadi, L; Bedouelle, Hugues (Apr 2014). "Direct and indirect interactions in the recognition between a cross-neutralizing antibody and the four serotypes of dengue virus".
1446:
Cornaby, Caleb; Gibbons, Lauren; Mayhew, Vera; Sloan, Chad S.; Welling, Andrew; Poole, Brian D. (2015). "B cell epitope spreading: Mechanisms and contribution to autoimmune diseases".
572:
299:
1027:
van Oss, CJ; Good, RJ; Chaudhury, MK (1986). "Nature of the antigen-antibody interaction. Primary and secondary bonds: optimal conditions for association and dissociation".
2000:
774:
Soluble antigens combine with soluble antibodies in presence of an electrolyte at suitable temperature and pH to form insoluble visible complex. This is called a
460:
328:
742:
Antigen-antibody interaction is used in laboratory techniques for serological test of blood compatibility and various pathogenic infections. The most basic is
814:
Goldberg, Richard J. (1952). "A Theory of
Antibody—Antigen Reactions. I. Theory for Reactions of Multivalent Antigen with Bivalent and Univalent Antibody".
76:
of the antibody, situated at the variable region of the polypeptide chain. The variable region in turn has hyper-variable regions which are unique
720:
for the interactions they describe. The lower the dissociation constant, the higher the avidity or affinity, and the stronger the interaction.
1348:"Exploring avidity: understanding the potential gains in functional affinity and target residence time of bivalent and heterobivalent ligands"
1703:
1625:
852:
1054:
Absolom, DR; van Oss, CJ (1986). "The nature of the antigen-antibody bond and the factors affecting its association and dissociation".
925:
992:
Mian, I.Saira; Bradwell, Arthur R.; Olson, Arthur J. (1991). "Structure, function and properties of antibody binding sites".
1690:, Techniques in Life Science and Biomedicine for the Non-Expert, Cham: Springer International Publishing, pp. 23–30,
563:
1550:
81:
775:
694:{\displaystyle K_{a}={\frac {k_{{\ce {on}}}}{k_{{\ce {off}}}}}={\frac {{\ce {}}}{{\ce { }}}}={\frac {r}{c(n-r)}}}
178:
93:
790:
190:
61:
209:
2025:
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1839:"Quantitation of Food Adulterants by Multiple Radial Immunodiffusion. I. Cross-Reacting Antigen Mixtures"
1297:
Estep, Patricia; Reid, Felicia; Nauman, Claire; Liu, Yuqi; Sun, Tingwan; Sun, Joanne; Xu, Yingda (2013).
763:
717:
69:
60:
The first correct description of the antigen-antibody reaction was given by
Richard J. Goldberg at the
89:
80:
in each antibody. Antigens are bound to antibodies through weak and noncovalent interactions such as
151:
called framework regions. Each V domain has four framework domains, namely FR1, FR2, FR3, and FR4.
2030:
2020:
186:
77:
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A special ring test is useful for diagnosis of anthrax and determination of adulteration in food.
121:
1979:
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1872:"Bubble-induced aggregation of platelets: effects of gas species, proteins, and decompression"
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1299:"High throughput solution-based measurement of antibody-antigen affinity and epitope binning"
552:{\displaystyle K_{d}={\frac {k_{{\ce {off}}}}{k_{{\ce {on}}}}}={\frac {{\ce { }}}{{\ce {}}}}}
420:{\displaystyle K_{a}={\frac {k_{{\ce {on}}}}{k_{{\ce {off}}}}}={\frac {{\ce {}}}{{\ce { }}}}}
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125:
Structural model of an antibody molecule. Rounded portions indicate antigen binding sites.
54:
1211:"Effects of antibody affinity and antigen valence on molecular forms of immune complexes"
17:
173:
Antibodies bind antigens through weak chemical interactions, and bonding is essentially
1927:
1902:
1800:"An immuno-diffusion assay to assess the protective antigen content of anthrax vaccine"
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in 1952. It came to be known as "Goldberg's theory" (of antigen-antibody reaction).
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The antibody-antigen binding kinetic can be described by the rate equation of a
133:
is formed from the amino-terminal end of both the light and heavy chains of the
912:
Janeway, Charles A Jr; Travers, Paul; Walport, Mark; Shlomchik, Mark J (2001).
708:
The overall strength of the binding of an antibody to an antigen is termed its
1950:
Parry, Christopher M.; Wijedoru, Lalith; Arjyal, Amit; Baker, Stephen (2011).
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1903:"Widal agglutination test – 100 years later: still plagued by controversy"
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1952:"The utility of diagnostic tests for enteric fever in endemic locations"
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are the association and dissociation rate constants, respectively.
751:
153:
120:
1757:"Double-immunodiffusion assay for detecting specific antibodies"
1524:"Immunoglobulins- antigen-antibody reactions and selected tests"
146:) creates three hypervariable regions (HV1, HV2, and HV3). In V
1397:"Binding Revisited-Avidity in Cellular Function and Signaling"
1483:"Assessing human B cell repertoire diversity and convergence"
159:
Discotope (light blue), ellipro (purple), and seppa (pink).
1870:
Thorsen, T.; Klausen, H.; Lie, R. T.; Holmsen, H. (1993).
870:"Goldberg's theory of antigen-antibody reactions in vitro"
1798:
Adams, Trudy; Osborn, Sancha; Rijpkema, Sjoerd (2005).
941:
Sela-Culang, Inbal; Kunik, Vered; Ofran, Yanay (2013).
729:
unexpected immune responses. This results in different
943:"The structural basis of antibody-antigen recognition"
916:
Immunobiology: The Immune System in Health and
Disease
447:
Reciprocally, the equilibibrium dissociation constant
260:
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463:
331:
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concentration, either in free (,) or bound () state.
212:
913:
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551:
419:
293:
1530:. University of South Carolina School of Medicine
1250:"Factors affecting the antigen-antibody reaction"
1162:"Factors affecting the antigen-antibody reaction"
268:
267:
250:
249:
1346:Vauquelin, Georges; Charlton, Steven J. (2013).
793:. They are used in blood tests for diagnosis of
1551:"Antigen/Antibody Tests for Infectious Disease"
1248:Reverberi, Roberto; Reverberi, Lorenzo (2007).
1160:Reverberi, Roberto; Reverberi, Lorenzo (2007).
1481:Imkeller, Katharina; Wardemann, Hedda (2018).
169:Chemical basis of antigen-antibody interaction
37:, is a specific chemical interaction between
8:
1684:"Precipitation and Agglutination Reactions"
1612:. Netherlands: Springer. pp. 309–386.
1254:Blood Transfusion = Trasfusione del Sangue
1166:Blood Transfusion = Trasfusione del Sangue
716:Avidity and affinity can be judged by the
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1395:Erlendsson, Simon; Teilum, Kaare (2020).
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920:(5 ed.). New York: Garland Science.
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1956:Expert Review of Anti-Infective Therapy
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1901:Olopoenia, L. A.; King, A. L. (2000).
294:{\displaystyle {\ce { + <=> }}}
131:Fab (fragment, antigen-binding) region
750:. Sophisticated applications include
315:The equilibrium association constant
7:
1647:Journal of Investigative Dermatology
1641:Odell, Ian D; Cook, Deborah (2013).
27:Immune response chemical interaction
1549:Margolis, Simeon (5 January 2012).
746:determination, which is useful for
1876:Undersea & Hyperbaric Medicine
1401:Frontiers in Molecular Biosciences
1056:CRC Critical Reviews in Immunology
847:. London: CRC Press. p. 257.
844:Applications of Percolation Theory
322:can therefore be represented as:
25:
564:second-order reversible reaction
72:or epitope is recognized by the
1761:Current Protocols in Immunology
1643:"Immunofluorescence Techniques"
1352:British Journal of Pharmacology
1682:Alhabbab, Rowa Yousef (2018),
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1843:Journal of AOAC International
1816:10.1016/j.vaccine.2005.04.017
754:, enzyme-linked immunospot (
142:) and variable heavy chain (V
31:Antigen-antibody interaction,
1907:Postgraduate Medical Journal
1769:10.1002/0471142735.im0203s00
1726:"Antigen-antibody reactions"
1618:10.1007/978-94-011-1552-0_12
1575:Immunological Investigations
1227:10.1016/j.molimm.2009.09.009
1139:10.1016/0031-6865(94)00046-x
1127:Pharmaceutica Acta Helvetiae
1006:10.1016/0022-2836(91)90617-F
994:Journal of Molecular Biology
1696:10.1007/978-3-319-77694-1_3
1610:Handbook of Immunochemistry
1608:FerenÄŤĂk, Miroslav (2013).
1528:Microbiology and Immunology
1460:10.1016/j.imlet.2014.11.001
198:Affinity of the interaction
2047:
1553:. Remedy Health Media, LLC
308:concentration and is the
179:Electrostatic interactions
82:electrostatic interactions
2001:Antigen-antibody reaction
1688:Basic Serological Testing
1587:10.3109/08820138309050753
1414:10.3389/fmolb.2020.615565
1029:Journal of Chromatography
841:Sahimi, Muhammad (1994).
35:antigen-antibody reaction
18:Antigen-antibody reaction
960:10.3389/fimmu.2013.00302
191:hydrophobic interactions
94:hydrophobic interactions
1837:Lietze, Arthur (1969).
1763:. Chapter 2: Unit 2.3.
947:Frontiers in Immunology
62:University of Wisconsin
1856:10.1093/jaoac/52.5.988
785:Agglutination reaction
776:precipitation reaction
770:Precipitation reaction
695:
553:
421:
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160:
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1919:10.1136/pmj.76.892.80
1755:Hornbeck, P. (2001).
1487:Immunological Reviews
764:immunoelectrophoresis
718:dissociation constant
696:
554:
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296:
157:
124:
70:antigenic determinant
1724:Virella, G. (1993).
1660:10.1038/jid.2012.455
1266:10.2450/2007.0047-07
1215:Molecular Immunology
1178:10.2450/2007.0047-07
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461:
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187:van der Waals forces
129:In an antibody, the
90:Van der Waals forces
78:amino acid sequences
868:Spiers, JA (1958).
828:10.1021/ja01142a045
731:autoimmune diseases
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1448:Immunology Letters
1315:10.4161/mabs.23049
760:immunofluorescence
724:Autoimmune disease
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117:Antibody structure
1968:10.1586/eri.11.47
1810:(36): 4517–4520.
1730:Immunology Series
1705:978-3-319-77693-4
1627:978-94-010-4678-7
1500:10.1111/imr.12670
1364:10.1111/bph.12106
854:978-0-203-22153-2
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401:
395:
388:
382:
375:
362:
350:
344:
339:
335:
318:
304:where is the
302:
301:
288:
282:
272:
265:
254:
247:
237:
231:
227:
223:
217:
199:
196:
183:hydrogen bonds
170:
167:
165:
162:
147:
143:
139:
135:immunoglobulin
118:
115:
109:
106:
100:microbes, and
86:hydrogen bonds
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
2043:
2032:
2029:
2027:
2026:Immune system
2024:
2022:
2019:
2018:
2016:
2007:
2004:
2002:
1999:
1998:
1994:
1985:
1981:
1977:
1973:
1969:
1965:
1961:
1957:
1953:
1946:
1943:
1938:
1934:
1929:
1924:
1920:
1916:
1912:
1908:
1904:
1897:
1894:
1889:
1885:
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1877:
1873:
1866:
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1857:
1852:
1848:
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1833:
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1825:
1821:
1817:
1813:
1809:
1805:
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1778:
1774:
1770:
1766:
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1758:
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1735:
1731:
1727:
1720:
1717:
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1697:
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1678:
1675:
1670:
1666:
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1656:
1652:
1648:
1644:
1637:
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1629:
1623:
1619:
1615:
1611:
1604:
1601:
1596:
1592:
1588:
1584:
1580:
1576:
1568:
1565:
1552:
1545:
1542:
1529:
1525:
1522:Mayer, Gene.
1518:
1515:
1510:
1506:
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1492:
1488:
1484:
1477:
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1465:
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1425:
1420:
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1398:
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1179:
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1136:
1133:(4): 225–30.
1132:
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1120:
1117:
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1108:
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1100:
1096:
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1088:
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1038:
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988:
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980:
976:
971:
966:
961:
956:
952:
948:
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937:
934:
929:
927:0-8153-3642-X
923:
918:
917:
908:
906:
902:
897:
893:
888:
883:
880:(2): 89–102.
879:
875:
871:
864:
861:
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850:
846:
845:
837:
834:
829:
825:
821:
817:
810:
807:
800:
798:
796:
795:enteric fever
792:
791:agglutination
784:
782:
779:
777:
769:
767:
765:
761:
757:
753:
749:
745:
737:
735:
732:
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714:
711:
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188:
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180:
176:
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156:
152:
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123:
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1709:, retrieved
1687:
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1609:
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1578:
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1567:
1555:. Retrieved
1544:
1532:. Retrieved
1527:
1517:
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1490:
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1451:
1447:
1441:
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1400:
1390:
1355:
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1302:
1292:
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175:non-covalent
172:
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34:
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1736:: 117–133.
1062:(1): 1–46.
738:Application
104:parasites.
2031:Hematology
2021:Immunology
2015:Categories
1711:2021-11-11
1407:: 615565.
874:Immunology
801:References
164:Properties
39:antibodies
1653:(1): e4.
1035:: 111–9.
680:−
454:will be:
271:⇀
264:−
253:−
246:↽
1976:21692675
1937:10644383
1824:15908061
1785:26865070
1777:18432768
1669:23299451
1557:10 March
1534:10 March
1509:29944762
1468:25445494
1433:33521057
1382:23330947
1333:23575269
1284:19204779
1235:19800690
1196:19204779
1103:24591178
979:24115948
896:13538526
306:antibody
102:helminth
74:paratope
51:antigens
1984:3414927
1928:1741491
1888:8392414
1804:Vaccine
1742:8424970
1595:6350166
1424:7841115
1373:3623049
1324:3893237
1275:2581910
1187:2581910
1147:7651966
1111:5416842
1068:3522103
1041:3711190
1014:1988675
970:3792396
953:: 302.
887:1423897
756:Elispot
710:avidity
310:antigen
53:during
45:of the
43:B cells
1982:
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851:
762:, and
430:where
189:, and
92:, and
1980:S2CID
1781:S2CID
1107:S2CID
752:ELISA
1972:PMID
1933:PMID
1884:PMID
1820:PMID
1773:PMID
1738:PMID
1700:ISBN
1665:PMID
1622:ISBN
1591:PMID
1559:2015
1536:2015
1505:PMID
1464:PMID
1429:PMID
1378:PMID
1329:PMID
1303:mAbs
1280:PMID
1231:PMID
1192:PMID
1143:PMID
1099:PMID
1064:PMID
1037:PMID
1010:PMID
975:PMID
922:ISBN
892:PMID
849:ISBN
628:AbAg
540:AbAg
437:and
384:AbAg
284:AbAg
49:and
1964:doi
1923:PMC
1915:doi
1851:doi
1812:doi
1765:doi
1692:doi
1655:doi
1651:133
1614:doi
1583:doi
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1491:284
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1368:PMC
1360:doi
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1270:PMC
1262:doi
1223:doi
1182:PMC
1174:doi
1135:doi
1091:doi
1033:376
1002:doi
998:217
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882:PMC
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610:off
486:off
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