ライフサイエンスコーパス: MSA-1

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1 two molecules, merozoite surface antigen 1 (MSA-1) and rhoptry-associated protein 1 (RAP-1), that ar

2 ely analyzed in merozoite surface antigen 1 (MSA-1) from 16 strains and isolates.

3 e Babesia bovis merozoite surface antigen 1 (MSA-1) is an immunodominant membrane glycoprotein that i

4 e Babesia bovis merozoite surface antigen 1 (MSA-1), a member of the variable merozoite surface antig

5 Although MSA-1 amino acid sequence varied substantially among str

6 to 1640); they were able to inhibit 2B10 and MSA-1 binding to erythrocytes and partially prevent P. f

7 rocyte receptors and their ligands, 2B10 and MSA-1, are related and that the C-terminal region of MSA

8 same determinant on the human erythrocyte as MSA-1 of Plasmodium falciparum (FCR3 strain); the bindin

9 identified the sequence differences between MSA-1 antigenically dissimilar strains.

10 2B10 in the study of the interaction between MSA-1 and human erythrocytes prompted us to determine th

11 a complete lack of cross-reactivity between MSA-1 from vaccine and breakthrough strains in immunized

12 Both MSA-1 and RAP-1 were transcribed and expressed in infect

13 respectively), in contrast to the extensive MSA-1 sequence variation (52% identity) between the same

14 , suggesting a conserved functional role for MSA-1 despite sequence polymorphism.

15 antigenic variation has been demonstrated in MSA-1 among strains from distinct geographical areas, th

16 e sequence variation in another VMSA member, MSA-1, has been shown in all vaccine breakthrough isolat

17 Importantly, monospecific MSA-1 and RAP-1 antisera each inhibited sporozoite invas

18 ng site of 2B10 and the C-terminal region of MSA-1 (amino acids 1047 to 1640); they were able to inhi

19 uences of the 2B10 VH region and a region of MSA-1 from the Wellcome strain of P. falciparum (amino a

20 re related and that the C-terminal region of MSA-1 is the erythrocyte binding domain.

21 ocyte invasion and suggest that selection of MSA-1 variants may be driven by invasion-blocking antibo

22 In this study, sequencing of MSA-1 from two Australian B. bovis vaccine strains and 1

23 a conserved functional role for polymorphic MSA-1 in erythrocyte invasion.

24 equence conservation, antibodies against R1A MSA-1 were able to inhibit invasion of erythrocytes by M

25 gainst S2P MSA-1 cross-react with native R1A MSA-1.

26 al to each other, and antibodies against S2P MSA-1 cross-react with native R1A MSA-1.

27 10 VL region and another segment of the same MSA-1 (amino acids 1247 to 1394) share 48% similarity.

28 The MSA-1 HVR is proline rich and contains three semiconserv

29 The results indicate that the MSA-1 HVR is involved in erythrocyte invasion and sugges

30 Two MSA-1-specific monoclonal antibodies previously shown to

31 e clinically immune did not cross-react with MSA-1 from any other isolate tested.

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