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The intraspecific and interspecific competition among the adults of three common grasshoppers, Angaracris rhodopa (Fischer-Waldheim), Chorthippus dubius (Zubovsky) and Chorthippus fallax (Zubovsky) was investigated on Ganjia High Mountain Grassland in north-west China. The results indicated a strong intraspecific competition within species at high densities. The interspecific competition between the larger-sized species, A. rhodopa, and the smaller-sized species, C. dubius or C. fallax, was weak, while competition between C. dubius and C. fallax was strong. An asymmetric competitive interaction in mortality and fecundity associated with the diet and size was observed among the three species. Competition was strong between the two species that had a similar diet. The large-sized species had higher mortality rates and lower fecundity than the smaller-sized species. Intraspecific competition between the three species was mainly affected by food limitation, while interspecific competition was mainly associated with food limitation as well as the grasshoppers’ adaptation to the environment. [ABSTRACT FROM AUTHOR]

As the national key discipline and the initiator of oral and maxillofacial deformity group, the Department of Oral and Maxillofacial Surgery persisted in teaching, designed a novel teaching form combining theoretical knowledge and online software practice according to the characteristics of our discipline and carried out "cloud training" via the National Oral Telemedicine Education Platform. Ten lecturers, 325 theoretical students and 50 practical students were investigated by questionnaire in the present study with questions focusing on the geographical distribution and composition of personnel, etc. The results showed that the online course covered a wide range of students and achieved high acceptance and satisfaction rate. The first online software operation course was conducted in an orderly manner, with timely interaction between teachers and students. The students were able to master the design process skillfully. This "cloud training" has achieved good results, but there are still a series of problems that have yet to be resolved, such as network stalls and protection of intellectual property rights. Under the new form, the exploration and analysis of the new mode of online telemedicine specialist education will provide some practical reference for the National Clinical Research Center for Oral Diseases to carry out online telemedicine teaching in the future.

Active immunization with myelin basic protein (MBP) induces experimental allergic encephalomyelitis (EAE) in a variety of animal species, including rats and mice. We have previously described the ability of the newly described mouse lambda (lambda) variable (V) region V lambda x, to confer MBP reactivity to an Ab. In this report, we have evaluated the heavy (H) chain isotype distribution of V lambda x-bearing Abs in normal mouse serum. We demonstrate a biased H chain isotype association with V lambda x light (L) chains with a skewing towards gamma 2a and 2b isotypes. The IgG2a restriction in normal mouse Igs is even more evident in V lambda x-containing Abs that bind MBP. This was confirmed by the ability of purified polyclonal IgG2a Abs to bind MBP and the finding that most or all of the IgG2a Abs that bind MBP seem to harbor a V lambda x L chain. The specificity of naturally-occurring V lambda x-bearing Abs with MBP can be localized to a particular epitope encompassing residues 25-34 of the MBP molecule. Furthermore, virtually all of the reactivity of V lambda x-containing Abs with MBP peptide 25-34 is associated with the gamma 2a isotype. Collectively, these results suggest that the interaction of V lambda x with MBP seems to be facilitated by an association with gamma 2a which may reflect preferred VH usage by this isotype. Such unique pairing of particular H chains with V lambda x L chains in Abs that bind MBP may be indicative of a new B-cell component involved in the pathogenesis of EAE.

Superantigens, such as staphylococcal enterotoxins, activate T lymphocytes by linking MHC class II molecules on antigen presenting cells to the V beta element of the TCR. Through this effect on T cells, superantigens may influence the immune response and autoimmune disease. In fact, superantigens may activate or anergize cells involved in the production of experimental allergic encephalomyelitis. Lewis rats recognize an encephalitogenic epitope in myelin basic protein (MBP) residues 68-88 through an MHC class II I-A restricted process using TCR V beta 8.2. The F30 murine mAb reacts with an encephalitogenic idiotope (Id) on the TCR of V beta 8.2+ encephalitogenic Lewis rat T cells. In the present study it was demonstrated that the same mAb anti-Id inhibited the proliferation and IL-2 secretion induced by staphylococcal enterotoxins A, B and E in a V beta 8.2+ encephalitogenic Lewis rat T cell line specific for guinea pig MBP peptide 68-88. The mAb anti-Id did not inhibit the response of control T cells similarly derived but inhibited V beta 8.2- and recognizing MBP peptide 87-99. Control anti-Id failed to inhibit the response of either cell line. These findings imply that the specific antigen and superantigen react with TCR in a manner similar enough to be inhibited by the same anti-Id. The mechanism may involve the induction of anergy by the anti-Id, interference/steric hindrance by the reaction of anti-Id with TCR and possibly a little direct reaction of anti-Id with superantigens. Anti-Id directed immunotherapy may have a role in modulating the damage of inflammatory demyelination induced by both specific antigens and superantigens.

We have written a computer program to aid in the identification of interaction sites between proteins. The program compares the hydropathic profiles of the two interacting proteins and reports sites, demonstrating an exact pattern of inverted hydropathy. If these regions are surface accessible in the folded proteins, they are considered putative binding or docking sites and can be tested as such. In this report, we apply this program to the localization of residues involved in the anti-idiotope of a monoclonal antibody (mAb), F30C7. The anti-idiotope of F30C7 partially resembles the structure of the peptide antigen, human myelin basic protein (MBP) acetyl 1-9, used to elicit the idiotope bearing mAbs (Ab1). The sequences of F30C7 variable regions are compared to the variable regions of Ab1, as well as to the peptide antigen used to elicit F30C7. Sites of hydropathic complementarity in F30C7 with Ab1 that also have sequential homology with MBP 1-9 were located, and a synthetic peptide designed from these sequences was found to structurally resemble MBP 1-9 in that it: (i) inhibited Ab1 binding to MBP 1-9 and (ii) partially inhibited the binding of F30C7 to Ab1. Thus the portion of the anti-idiotope of F30C7 resembling MBP 1-9 was determined with the aid of this program. Other hits between F30C7 and Ab1 also occurred, and future studies will determine whether or not these sites might further contribute to the anti-idiotope.

In this article we review the field of idiotype (Id) network and experimental allergic encephalomyelitis, focusing on the generation of monoclonal antibody anti-Id by using complementary peptide and the investigation of anti-Id immunoregulatory effects on immune responses of B and T cells to specific myelin basic protein peptides in vitro and in vivo.

The present study was undertaken to compare the features of monoclonal antibody (mAb) anti-idiotope (Id) induced by complementary peptides, synthesized on the basis of inverted hydropathy for a myelin basic protein (MBP) peptide, or by conventional methodology using Id-bearing antibodies to the same MBP peptide as immunogen. The six reagents studied consisted of mAbs reactive with MBP peptide acetyl 1-9 and MBP peptide 80-89 and anti-Id reagents against these two mAbs prepared by either the complementary peptide or the conventional approach. ELISA, immunoblotting, immunoinhibition of hybridoma cell production of Id-bearing mAb to MBP, and FACS indicated that the anti-Ids generated by either technique were similar although existing in a range reflecting biologic phenomena. mAbs anti-Id prepared by either method continued to show an IgM isotype preference, possibly related to technical considerations, and continued to recognize a cross-reactive Id on the kappa light chain of the mAbs to MBP peptides acetyl 1-9 and 80-89. There was no indication that the anti-Ids prepared by the complementary peptide approach were restrictive or selective in a manner different from those made by the conventional approach.

In order to assess the role of idiotype (Id) and the anti-Id network in murine experimental autoimmune encephalomyelitis (EAE), Id-bearing monoclonal antibodies (mAb) to human myelin basic protein (MBP) peptide acetyl 1-9, as well as mAb anti-Id, were developed in EAE-susceptible PL/J mice (H-2u). These mice recognize MBP residues acetyl 1-9 as an encephalitogenic determinant. Reactivities of PL/J Id-bearing mAbs to MBP and to MBP peptides were identical to those of mAbs generated against the same MBP peptide in EAE-resistant BALB/c mice (H-2d), even though isotypes of the mAbs differed. By using an inhibitory ELISA and immunoblotting, it was demonstrated that one PL/J mAb anti-Id recognized a public or framework Id, whereas another PL/J mAb-anti Id was directed to a private Id more restricted to the paratopic site. Two Id-bearing PL/J mAbs shared a cross-reactive Id (IdX) on the light chain, and an interstrain IdX was present on both the heavy and light chains of mAbs raised in PL/J and BALB/c mice to the same MBP peptide. The PL/J mAb anti-Id was capable of cross-regulating the production of Id-bearing mAbs by hybridomas across murine strains. These findings suggest that a restrictive family of germ-line genes encode for these Id-bearing antibodies to MBP peptide, irrespective of whether the MBP peptide is encephalitogenic in the murine strain immunized. Manipulation of the Id network may provide a means for modifying autoimmune demyelinating diseases of the central nervous system.

An immunochemical analysis was conducted to compare the C1 isomer of human myelin basic protein (MBP) with the newly described and less cationic, citrullinated isomer of MBP referred to as C8. Ten polyclonal antisera directed at multiple epitopes or restricted regions of MBP were used in radioimmunoassays to examine MBP-C1 and MBP-C8. Antisera reactive with MBP peptide 1-14 clearly distinguished MBP-C1 from MBP-C8. Antisera to human MBP peptides 10-19 and 90-170, but not to MBP peptide 69-89, showed modest differences between MBP-C1 and MBP-C8. The MBP-C8s from multiple sclerosis (MS) and non-MS brain reacted essentially the same. With murine monoclonal antibodies and enzyme-linked immunosorbent assay (ELISA), differences between MBP-C8 and other isomers were shown for anti-MBP 10-19 but not for anti-MBP 1-9 or anti-MBP 80-89. These findings imply differences in sequence or conformation in the structure of MBP-C7 compared to MBP-C1, most notably near the amino terminus.

The idiotype (ID) of an antibody is postulated to be involved in immunoregulation by means of the immune network. This hypothesis was examined by studying the effect of a monoclonal antibody (MAb) anti-ID on hybridoma cells secreting an ID-bearing MAb, 845D3, to human myelin basic protein (MBP) peptide 80-89. The monoclonal anti-ID (IgM/kappa), reacted with heavy and light chains of 845D3, an IgG1/kappa MAb, but not with a control MAb of the same isotype specific for an MBP peptide differing by one amino acid residue. Fluorescence-activated cell sorting revealed IgG heavy and kappa light chains on the surface and in the cytoplasm of 90% or more of the 845D3 cells. The anti-ID did not react with the surface of the 845D3-secreting cells, and reacted with the cytoplasm of 14-18% of these cells. In spite of the absence of cell surface ID, the anti-ID significantly decreased antibody production by the ID-secreting cells. There was no effect of the anti-ID on control hybridoma cells secreting MAb to another MBP cells. There was no effect of the anti-ID on control hybridoma cells secreting MAb to another MBP peptide. Anti-ID exerted no cytotoxic effect on ID-bearing hybridoma cells and in fact caused a marginal increase in their proliferation compared to control MAb. These results indicate that an anti-ID may alter the antibody production of ID-secreting cells in a specific manner and without cytotoxicity. This may be one of the means for controlling an immune response against MBP generated by the cells of the immune system or in situ within the nervous system. The cellular mechanism(s) for this effect remains to be defined.

Pelvic fractures with or without dislocation in 105 females, aged above 15 years, were studied. 47.6% of the fractures was through the antero-posterior ring. Among the complications, genital organ injury happened in 15 patients (14.5%): rupture of uterus in 5 (3 wombs conceived over 3 mon, 1 in period of nursing, 1 in normal state), rupture of ovary in 2, rupture of ovarian tube in 1 and laceration of vagina in 7. They were treated accordingly in urgent need. Follow-up of 1 to 5 years, averaging 5.3 years, showed various sequelae related to original pelvic trauma, of which accounts were given. It is worthy to emphasize that 45 of 75 patients (60%), who had become pregnant later, experienced dystocia due either to deformed pelvis or contracted vagina. 30 of the 45 patients had to undergo cesarean section. 15 other patients (14.3%) became barren following pelvic trauma, though they expected to be mother. Causes of the secondary sterility were discussed. Some patients experienced difficulty in sexual activity because of spoiled vagina, being involved by displaced bone fragment intrusion or by cicatricial contracture of itself. In short, in view of obstetrics, displaced pelvic fracture--dislocation should be reduced early following resuscitation of the patient, and be maintained steady by traction until union or by internal fixation if needed.